{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T04:37:25Z","timestamp":1779338245597,"version":"3.51.4"},"reference-count":58,"publisher":"Elsevier BV","issue":"1-2","license":[{"start":{"date-parts":[[2000,10,1]],"date-time":"2000-10-01T00:00:00Z","timestamp":970358400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology"],"published-print":{"date-parts":[[2000,10]]},"DOI":"10.1016\/s0167-4838(00)00148-5","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T14:34:17Z","timestamp":1027607657000},"page":"9-24","source":"Crossref","is-referenced-by-count":688,"title":["The lipocalin protein family: structural and sequence overview"],"prefix":"10.1016","volume":"1482","author":[{"given":"Darren R.","family":"Flower","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anthony C.T.","family":"North","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clare E.","family":"Sansom","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/S0167-4838(00)00148-5_BIB1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3180001","article-title":"The lipocalin protein family: structure and function","volume":"318","author":"Flower","year":"1996","journal-title":"Biochem. J."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB2","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0006-291X(05)81256-2","article-title":"Mouse oncogene protein-24p3 is a member of the lipocalin protein family","volume":"180","author":"Flower","year":"1991","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB3","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1002\/pro.5560020507","article-title":"Structure and sequence relationships in the lipocalins and related proteins","volume":"2","author":"Flower","year":"1993","journal-title":"Protein Sci."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB4","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1002\/prot.340080108","article-title":"Crystallographic refinement of human serum retinol binding-protein at 2 angstroms resolution","volume":"8","author":"Cowan","year":"1990","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB5","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/S0969-2126(97)00205-0","article-title":"Bovine beta-lactoglobulin at 1.8 angstrom resolution \u2013 still an enigmatic lipocalin","volume":"5","author":"Brownlow","year":"1997","journal-title":"Structure"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB6","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1002\/j.1460-2075.1987.tb02401.x","article-title":"the molecular structure of insecticyanin from the tobacco hornworm Manduca sexta L. at 2.6 \u00c5 resolution","volume":"6","author":"Holden","year":"1987","journal-title":"EMBO J."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB7","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/0022-2836(87)90296-8","article-title":"Molecular structure of the bilin binding-protein (BBP) from Pieris brassicae after refinement at 2.0-\u00c5 resolution","volume":"198","author":"Huber","year":"1987","journal-title":"J. Mole. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB8","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/360186a0","article-title":"Pheromone binding to 2 rodent urinary proteins revealed by X-ray crystallography","volume":"360","author":"Bocskei","year":"1992","journal-title":"Nature"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB9","first-page":"753","article-title":"The structures of \u03b12u-globulin and its complex with a hyaline droplet inducer","volume":"D55","author":"Chaudhuri","year":"1999","journal-title":"Acta Cryst."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB10","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/0969-2126(93)90004-Z","article-title":"Structure of the epididymal retinoic acid-binding protein at 2.1 angstrom resolution","volume":"1","author":"Newcomer","year":"1993","journal-title":"Structure"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB11","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1006\/jmbi.1999.2755","article-title":"The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin","volume":"289","author":"Coles","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB12","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1038\/nsb1096-863","article-title":"Domain swapping creates a third putative combining site in bovine odorant binding protein dimer","volume":"3","author":"Tegoni","year":"1996","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB13","doi-asserted-by":"crossref","first-page":"7913","DOI":"10.1021\/bi980179e","article-title":"The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism","volume":"37","author":"Spinelli","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB14","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1074\/jbc.274.4.2337","article-title":"Probing the molecular basis of allergy \u2013 three-dimensional structure of the bovine lipocalin allergen bos D 2","volume":"274","author":"Rouvinen","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB15","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1016\/S0969-2126(98)00131-2","article-title":"The crystal structure of nitrophorin 4 at 1.5 angstrom resolution: transport of nitric oxide by a lipocalin-based heme protein","volume":"6","author":"Andersen","year":"1998","journal-title":"Structure"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB16","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1016\/S1097-2765(00)80359-7","article-title":"Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure","volume":"3","author":"Paesen","year":"1999","journal-title":"Mol. Cell"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB17","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1002\/jmr.300080304","article-title":"Multiple molecular recognition properties of the lipocalin protein family","volume":"8","author":"Flower","year":"1995","journal-title":"J. Mol. Recogn."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB18","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0014-5793(93)80382-5","article-title":"Structural relationship of streptavidin to the calycin protein superfamily","volume":"333","author":"Flower","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB19","doi-asserted-by":"crossref","first-page":"11845","DOI":"10.1073\/pnas.94.22.11845","article-title":"Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug","volume":"94","author":"Fuentesprior","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB20","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/S0065-3233(08)60639-7","article-title":"Lipid-binding proteins \u2013 a family of fatty-acid and retinoid transport proteins","volume":"45","author":"Banaszak","year":"1994","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB21","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/0076-6879(90)84259-J","article-title":"Avidin and streptavidin","volume":"184","author":"Green","year":"1990","journal-title":"Methods Enzymol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB22","doi-asserted-by":"crossref","first-page":"653","DOI":"10.1006\/jmbi.1995.0249","article-title":"Crystal-structure of a complex between Serratia marcescens metalloprotease and an inhibitor from Erwinia chrysanthemi","volume":"248","author":"Baumann","year":"1995","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB23","doi-asserted-by":"crossref","first-page":"1837","DOI":"10.1074\/jbc.272.3.1837","article-title":"The salivary lipocalin Von Ebner\u2019s gland protein is a cysteine proteinase inhibitor","volume":"272","author":"Vanthof","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB24","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1016\/S0959-440X(98)80073-0","article-title":"How far divergent evolution goes in proteins","volume":"8","author":"Murzin","year":"1998","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB25","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1093\/protein\/11.9.723","article-title":"A topological nomenclature for protein structure","volume":"11","author":"Flower","year":"1998","journal-title":"Protein Eng."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB26","doi-asserted-by":"crossref","first-page":"4349","DOI":"10.1021\/bi952859c","article-title":"A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase","volume":"3","author":"Larsen","year":"1996","journal-title":"Biochemistry"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB27","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1006\/jmbi.1999.2973","article-title":"Phosphatidylinositol phosphate kinase: a link between protein kinase and glutathione synthase folds","volume":"291","author":"Grishin","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB28","doi-asserted-by":"crossref","first-page":"341","DOI":"10.2174\/092986650202220524125827","article-title":"A structural signature characteristic of the calycin protein superfamily","volume":"2","author":"Flower","year":"1995","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB29","doi-asserted-by":"crossref","first-page":"6278","DOI":"10.1021\/bi00019a004","article-title":"1.4 Angstrom structure of photoactive yellow protein, a cytosolic photoreceptor - unusual fold, active-site, and chromophore","volume":"34","author":"Borgstahl","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB30","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1073\/pnas.95.7.3413","article-title":"Crystal structure of MTCP-1: implications for role of TCL-1 and MTCP-1 in T cell malignancies","volume":"95","author":"Fu","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB31","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1093\/protein\/9.2.107","article-title":"A novel binding site in catalase is suggested by structural similarity to the calycin superfamily","volume":"9","author":"Russell","year":"1997","journal-title":"Protein Eng."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB32","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1038\/353276a0","article-title":"Structure of human cyclophilin and its binding-site for cyclosporine-A determined by X-ray crystallography and NMR-spectroscopy","volume":"353","author":"Kallen","year":"1991","journal-title":"Nature"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB33","doi-asserted-by":"crossref","first-page":"1977","DOI":"10.1002\/pro.5560041003","article-title":"Structural similarity between the pleckstrin homology domain and verotoxin \u2013 the problem of measuring and evaluating structural similarity","volume":"4","author":"Orengo","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB34","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0014-5793(97)00296-2","article-title":"A structural tree for proteins containing 3 beta-corners","volume":"407","author":"Efimov","year":"1997","journal-title":"FEBS Lett."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB35","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/S0022-2836(05)80134-2","article-title":"Scop: a structural classification of proteins database for the investigation of sequences and structures","volume":"247","author":"Murzin","year":"1995","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB36","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1242\/dev.121.1.135","article-title":"Developmental expression of the lipocalin lazarillo and its role in axonal pathfinding in the grasshopper embryo","volume":"121","author":"Sanchez","year":"1995","journal-title":"Development"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB37","doi-asserted-by":"crossref","first-page":"31196","DOI":"10.1074\/jbc.270.52.31196","article-title":"Cloning of cockroach allergen, Bla G 4, identifies ligand binding proteins (or calycins) as a cause of IgE antibody responses","volume":"270","author":"Arruda","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB38","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1111\/j.1432-1033.1991.tb16340.x","article-title":"Complete sequence and model for the C1 subunit of the carotenoprotein, crustacyanin, and model for the dimer, beta-crustacyanin, formed from the C1 and A2 subunits with astaxanthin","volume":"202","author":"Keen","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB39","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/S0014-5793(99)00414-7","article-title":"cDNA cloning of an adult male putative lipocalin specific to tergal gland aphrodisiac secretion in an insect (Leucophaea maderae)","volume":"449","author":"Korchi","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB40","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1016\/S0968-0004(00)89116-1","article-title":"The first prokaryotic lipocalins","volume":"20","author":"Flower","year":"1995","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB41","doi-asserted-by":"crossref","first-page":"23097","DOI":"10.1074\/jbc.270.39.23097","article-title":"Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins","volume":"270","author":"Bishop","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB42","doi-asserted-by":"crossref","first-page":"15321","DOI":"10.1074\/jbc.273.25.15321","article-title":"Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants","volume":"273","author":"Bugos","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB43","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1093\/oxfordjournals.molbev.a026224","article-title":"A Phylogenetic analysis of the lipocalin protein family","volume":"17","author":"Ganfornina","year":"2000","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB44","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/S0167-4838(00)00151-5","article-title":"Evolution of the lipocalin family as inferred from a protein sequence phylogeny","volume":"1482","author":"Guti\u00e9rrez","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB45","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0167-4838(00)00138-2","article-title":"The bacterial lipocalins","volume":"1482","author":"Bishop","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB46","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1999.2827","article-title":"Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer","volume":"289","author":"Ponting","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB47","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/S0962-8924(99)01664-5","article-title":"Lateral genomics","volume":"9","author":"Doolittle","year":"1999","journal-title":"Trends Cell Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB48","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1006\/jmbi.1994.1312","article-title":"Many of the immunoglobulin superfamily domains in cell-adhesion molecules and surface-receptors belong to a new structural set which is close to that containing variable domains","volume":"238","author":"Harpaz","year":"1994","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB49","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1093\/nar\/27.1.215","article-title":"The PROSITE database, its status in 1999","volume":"27","author":"Hofmann","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB50","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1021\/ci960468e","article-title":"The PRINTS database of protein fingerprints: a novel information resource for computational molecular biology","volume":"37","author":"Attwood","year":"1997","journal-title":"J. Chem. Inf. Comput. Sci."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB51","doi-asserted-by":"crossref","first-page":"304","DOI":"10.1093\/nar\/26.1.304","article-title":"The PRINTS protein fingerprint database in its fifth year","volume":"26","author":"Attwood","year":"1998","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB52","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1093\/nar\/27.1.220","article-title":"PRINTS prepares for the new millennium","volume":"27","author":"Attwood","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB53","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1093\/nar\/28.1.225","article-title":"PRINTS-S: the database formerly known as PRINTS","volume":"28","author":"Attwood","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB54","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1006\/jmbi.1998.2043","article-title":"Supersites within superfolds. Binding site similarity in the absence of homology","volume":"282","author":"Russell","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB55","first-page":"207","article-title":"Modelling G protein coupled receptors for drug design","volume":"1422","author":"Flower","year":"1999","journal-title":"Rev. Biomembr."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB56","doi-asserted-by":"crossref","first-page":"S19","DOI":"10.1016\/S1359-0278(97)00059-X","article-title":"Protein structures sustain evolutionary drift","volume":"2","author":"Rost","year":"1997","journal-title":"Fold. Design"},{"key":"10.1016\/S0167-4838(00)00148-5_BIB57","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S1093-3263(97)00101-0","article-title":"ALTER: eclectic management of molecular structure data","volume":"15","author":"Flower","year":"1997","journal-title":"J. Mol. Graph. Mod."},{"key":"10.1016\/S0167-4838(00)00148-5_BIB58","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1002\/(SICI)1097-0134(19990215)34:3<341::AID-PROT7>3.0.CO;2-Z","article-title":"Finding local structural similarities among families of unrelated protein structures: A generic non-linear alignment algorithm","volume":"34","author":"Lehtonen","year":"1999","journal-title":"Proteins"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167483800001485?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167483800001485?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2023,4,9]],"date-time":"2023-04-09T09:04:35Z","timestamp":1681031075000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0167483800001485"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2000,10]]},"references-count":58,"journal-issue":{"issue":"1-2","published-print":{"date-parts":[[2000,10]]}},"alternative-id":["S0167483800001485"],"URL":"https:\/\/doi.org\/10.1016\/s0167-4838(00)00148-5","relation":{},"ISSN":["0167-4838"],"issn-type":[{"value":"0167-4838","type":"print"}],"subject":[],"published":{"date-parts":[[2000,10]]}}}