{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T17:19:08Z","timestamp":1788283148643,"version":"build-2803163510"},"reference-count":57,"publisher":"American Chemical Society (ACS)","issue":"32","license":[{"start":{"date-parts":[[2015,7,28]],"date-time":"2015-07-28T00:00:00Z","timestamp":1438041600000},"content-version":"vor","delay-in-days":365,"URL":"https:\/\/pubs.acs.org\/page\/policy\/authorchoice_termsofuse.html"}],"funder":[{"DOI":"10.13039\/100004863","name":"New York State Foundation for Science, Technology and Innovation","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/100004863","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/na","name":"Biotechnology Research and Development Corporation","doi-asserted-by":"publisher","award":["NA"],"award-info":[{"award-number":["NA"]}],"id":[{"id":"10.13039\/na","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,8,19]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>A number of surface proteins specific to pathogenic strains of Leptospira have been identified. The Lig protein family has shown promise as a marker in typing leptospiral isolates for pathogenesis and as an antigen in vaccines. We used NMR spectroscopy to solve the solution structure of the twelfth immunoglobulin-like (Ig-like) repeat domain from LigB (LigB-12). The fold is similar to that of other bacterial Ig-like domains and comprised mainly of \u03b2-strands that form a \u03b2-sandwich based on a Greek-key folding arrangement. Based on sequence analysis and conservation of structurally important residues, homology models for the other LigB Ig-like domains were generated. The set of LigB models illustrates the electrostatic differences between the domains as well as the possible interactions between neighboring domains. Understanding the structure of the extracellular portion of LigB and related proteins is important for developing diagnostic methods and new therapeutics directed toward leptospirosis.<\/jats:p>","DOI":"10.1021\/bi500669u","type":"journal-article","created":{"date-parts":[[2014,7,28]],"date-time":"2014-07-28T15:38:22Z","timestamp":1406561902000},"page":"5249-5260","source":"Crossref","is-referenced-by-count":23,"title":["NMR Solution Structure of the Terminal Immunoglobulin-like\nDomain from the\n                    <i>Leptospira<\/i>\n                    Host-Interacting Outer\nMembrane Protein, LigB"],"prefix":"10.1021","volume":"53","author":[{"given":"Christopher P.","family":"Ptak","sequence":"first","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14853"]},{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14853"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ching-Lin","family":"Hsieh","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14853"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi-Pin","family":"Lin","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14853"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander S.","family":"Maltsev","sequence":"additional","affiliation":[{"name":"National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health , , , ,","place":["Bethesda, Maryland, United States, 20892-0520"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajeev","family":"Raman","sequence":"additional","affiliation":[{"name":"Center for Cellular and Molecular Biology , Uppal Road , ,","place":["Hyderabad, India, 500 007"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yogendra","family":"Sharma","sequence":"additional","affiliation":[{"name":"Center for Cellular and Molecular Biology , Uppal Road , ,","place":["Hyderabad, India, 500 007"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert E.","family":"Oswald","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14853"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yung-Fu","family":"Chang","sequence":"additional","affiliation":[{"name":"Cornell University , , , ,","place":["Ithaca, New York, United States, 14853"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2014,7,28]]},"reference":[{"key":"2026090112462969300_cit1","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1097\/QCO.0b013e32814a5729","article-title":"Leptospirosis: Pathogenesis, immunity,\nand diagnosis","volume":"20","author":"Palaniappan","year":"2007","journal-title":"Curr. 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Dis."},{"key":"2026090112462969300_cit4","doi-asserted-by":"crossref","first-page":"406","DOI":"10.3201\/eid1003.030431","article-title":"Reemerging\nleptospirosis, California","volume":"10","author":"Meites","year":"2004","journal-title":"Emerging Infect.\nDis."},{"key":"2026090112462969300_cit5","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1111\/j.1365-2958.1993.tb01729.x","article-title":"Bacterial\nproteins binding to the mammalian extracellular-matix","volume":"9","author":"Westerlund","year":"1993","journal-title":"Mol. Microbiol."},{"key":"2026090112462969300_cit6","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1038\/nrmicro2208","article-title":"Leptospira: The dawn of the molecular\ngenetics era for an emerging zoonotic pathogen","volume":"7","author":"Ko","year":"2009","journal-title":"Nat. Rev. Microbiol."},{"key":"2026090112462969300_cit7","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/j.jmb.2009.05.034","article-title":"Structure\nand Calcium-Binding Activity of LipL32, the Major Surface Antigen\nof Pathogenic Leptospira sp","volume":"390","author":"Hauk","year":"2009","journal-title":"J. Mol. Biol."},{"key":"2026090112462969300_cit8","doi-asserted-by":"crossref","first-page":"3245","DOI":"10.1074\/jbc.M109.006320","article-title":"Calcium\nBinds to LipL32, a Lipoprotein from Pathogenic Leptospira, and Modulates\nFibronectin Binding","volume":"285","author":"Tung","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2026090112462969300_cit9","doi-asserted-by":"crossref","first-page":"1229","DOI":"10.1016\/j.jmb.2009.02.038","article-title":"Crystal Structure of\nLipL32, the Most Abundant Surface Protein of Pathogenic Leptospira\nspp","volume":"387","author":"Vivian","year":"2009","journal-title":"J. Mol. 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Chem."},{"key":"2026090112462969300_cit17","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0011301","article-title":"The Terminal Immunoglobulin-Like\nRepeats of LigA and LigB of Leptospira Enhance Their Binding to Gelatin\nBinding Domain of Fibronectin and Host Cells","volume":"5","author":"Lin","year":"2010","journal-title":"PLoS One"},{"key":"2026090112462969300_cit18","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1016\/j.bbrc.2007.07.196","article-title":"A domain of the\nLeptospira LigB contributes to high\naffinity binding of fibronectin","volume":"362","author":"Lin","year":"2007","journal-title":"Biochem. Biophys.\nRes. Commun."},{"key":"2026090112462969300_cit19","doi-asserted-by":"crossref","first-page":"19380","DOI":"10.1074\/jbc.M109.004531","article-title":"Repeated Domains\nof Leptospira Immunoglobulin-like\nProteins Interact with Elastin and Tropoelastin","volume":"284","author":"Lin","year":"2009","journal-title":"J. Biol. 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Biol."},{"key":"2026090112462969300_cit28","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1038\/emboj.2010.57","article-title":"Crystal structure of the yeast Sac1: Implications for\nits phosphoinositide phosphatase function","volume":"29","author":"Manford","year":"2010","journal-title":"EMBO\nJ."},{"key":"2026090112462969300_cit29","volume-title":"Molecular\nCloning: A Laboratory Manual","author":"Maniatis","year":"1982"},{"key":"2026090112462969300_cit30","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S0076-6879(72)25041-8","article-title":"Reaction\nof protein sulfhydryl groups with Ellman\u2019s reagent","volume":"25","author":"Habeeb","year":"1972","journal-title":"Methods Enzymol."},{"key":"2026090112462969300_cit31","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1023\/A:1012417721455","article-title":"Controlling residual dipolar couplings\nin high-resolution NMR of proteins by strain induced alignment in\na gel","volume":"21","author":"Ishii","year":"2001","journal-title":"J. Biomol. NMR"},{"key":"2026090112462969300_cit32","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A multidimensional spectral\nprocessing system based on UNIX\npipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"2026090112462969300_cit33","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pcbi.1000307","article-title":"Probabilistic\nInteraction Network of Evidence Algorithm and its Application to Complete\nLabeling of Peak Lists from Protein NMR Spectroscopy","volume":"5","author":"Bahrami","year":"2009","journal-title":"PLoS Comput. Biol."},{"key":"2026090112462969300_cit34","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S1090-7807(02)00014-9","article-title":"The Xplor-NIH NMR\nmolecular structure determination package","volume":"160","author":"Schwieters","year":"2003","journal-title":"J.\nMagn. Reson."},{"key":"2026090112462969300_cit35","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s10858-009-9395-y","article-title":"Prediction of Xaa-Pro\npeptide bond conformation from sequence and\nchemical shifts","volume":"46","author":"Shen","year":"2010","journal-title":"J. Biomol. NMR"},{"key":"2026090112462969300_cit36","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1007\/s10858-013-9741-y","article-title":"Protein backbone and\nsidechain torsion angles predicted from NMR\nchemical shifts using artificial neural networks","volume":"56","author":"Shen","year":"2013","journal-title":"J. Biomol. NMR"},{"key":"2026090112462969300_cit37","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1007\/BF00228148","article-title":"AQUA and\nPROCHECK-NMR: Programs for checking the quality of protein structures\nsolved by NMR","volume":"8","author":"Laskowski","year":"1996","journal-title":"J. Biomol. NMR"},{"key":"2026090112462969300_cit38","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: All-atom structure validation\nfor macromolecular\ncrystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr., Sect. D:\nBiol. Crystallogr."},{"key":"2026090112462969300_cit39","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1002\/prot.21165","article-title":"Evaluating protein structures determined\nby structural genomics consortia","volume":"66","author":"Bhattacharya","year":"2007","journal-title":"Proteins:\nStruct., Funct., Bioinf."},{"key":"2026090112462969300_cit40","doi-asserted-by":"crossref","first-page":"W590","DOI":"10.1093\/nar\/gkh477","article-title":"SuperPose: A simple\nserver for sophisticated structural superposition","volume":"32","author":"Maiti","year":"2004","journal-title":"Nucleic Acids Res."},{"key":"2026090112462969300_cit41","doi-asserted-by":"crossref","first-page":"W29","DOI":"10.1093\/nar\/gkr367","article-title":"HMMER web server: Interactive sequence\nsimilarity searching","volume":"39","author":"Finn","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"2026090112462969300_cit42","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1006\/jmbi.1993.1626","article-title":"Comparative protein\nmodelling by satisfaction of spatial\nrestraints","volume":"234","author":"Sali","year":"1993","journal-title":"J. Mol. Biol."},{"key":"2026090112462969300_cit43","doi-asserted-by":"crossref","first-page":"3784","DOI":"10.1093\/nar\/gkg563","article-title":"ExPASy: The proteomics server for\nin-depth protein\nknowledge and analysis","volume":"31","author":"Gasteiger","year":"2003","journal-title":"Nucleic Acids Res."},{"key":"2026090112462969300_cit44","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1126\/science.7761829","article-title":"Classical electrostatics\nin biology and chemistry","volume":"268","author":"Honig","year":"1995","journal-title":"Science"},{"key":"2026090112462969300_cit45","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.meegid.2008.10.012","article-title":"Genetic\ndiversity of the Leptospiral immunoglobulin-like (Lig) genes in pathogenic\nLeptospira spp","volume":"9","author":"McBride","year":"2009","journal-title":"Infect. Genet. Evol."},{"key":"2026090112462969300_cit46","unstructured":"Aramini, J. M., Wang, D., Ciccosanti, C. T., Janjua, H., Rost, B., Acton, T. B., Xiao, R., Swapna, G. V. T., Everett, J. K., Montelione, G. T., and Northeast Structural Genomics Consortium.. Solution NMR structure of a Bacterial\nIg-like (Big_3) domain from Bacillus cereus: Northeast Structural\nGenomics Consortium target BcR147A. Manuscript in\npreparation, 2014."},{"key":"2026090112462969300_cit47","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.1038\/srep01079","article-title":"Solution structure\nof the Big domain from Streptococcus pneumoniae reveals a novel Ca2+-binding\nmodule","volume":"3","author":"Wang","year":"2013","journal-title":"Sci. Rep."},{"key":"2026090112462969300_cit48","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/S0092-8674(00)81002-8","article-title":"2.0 angstrom crystal structure of\na four-domain segment of human fibronectin encompassing the RGD loop\nand synergy region","volume":"84","author":"Leahy","year":"1996","journal-title":"Cell"},{"key":"2026090112462969300_cit49","doi-asserted-by":"crossref","first-page":"735","DOI":"10.1016\/j.jmb.2011.10.029","article-title":"Human Cardiac\nMyosin Binding Protein\nC: Structural Flexibility within an Extended Modular Architecture","volume":"414","author":"Jeffries","year":"2011","journal-title":"J. Mol. Biol."},{"key":"2026090112462969300_cit50","doi-asserted-by":"crossref","first-page":"2441","DOI":"10.1128\/IAI.01635-06","article-title":"Physiological osmotic induction of Leptospira interrogans\nadhesion: LigA and LigB bind extracellular matrix proteins and fibrinogen","volume":"75","author":"Choy","year":"2007","journal-title":"Infect. Immun."},{"key":"2026090112462969300_cit51","doi-asserted-by":"crossref","first-page":"1569","DOI":"10.1016\/j.bpj.2009.07.009","article-title":"Selective Filtering of Particles\nby the Extracellular Matrix: An Electrostatic Bandpass","volume":"97","author":"Lieleg","year":"2009","journal-title":"Biophys. J."},{"key":"2026090112462969300_cit52","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0016879","article-title":"The Multifunctional LigB Adhesin Binds Homeostatic\nProteins with Potential Roles in Cutaneous Infection by Pathogenic\nLeptospira interrogans","volume":"6","author":"Choy","year":"2011","journal-title":"PLoS One"},{"key":"2026090112462969300_cit53","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.jmb.2010.06.011","article-title":"The Structure of the\nFnIII Tandem A77-A78 Points to a Periodically Conserved Architecture\nin the Myosin-Binding Region of Titin","volume":"401","author":"Bucher","year":"2010","journal-title":"J. Mol.\nBiol."},{"key":"2026090112462969300_cit54","doi-asserted-by":"crossref","first-page":"D211","DOI":"10.1093\/nar\/gkp985","article-title":"The Pfam protein\nfamilies database","volume":"38","author":"Finn","year":"2010","journal-title":"Nucleic Acids Res."},{"key":"2026090112462969300_cit55","doi-asserted-by":"crossref","first-page":"4589","DOI":"10.1021\/bi400128r","article-title":"The Perturbation of\nTryptophan Fluorescence by Phenylalanine\nto Alanine Mutations Identifies the Hydrophobic Core in a Subset of\nBacterial Ig-like Domains","volume":"52","author":"Raman","year":"2013","journal-title":"Biochemistry"},{"key":"2026090112462969300_cit56","doi-asserted-by":"crossref","first-page":"1735","DOI":"10.1016\/S0006-3495(01)75825-0","article-title":"Decomposition of protein tryptophan\nfluorescence spectra into log-normal components. III. Correlation\nbetween fluorescence and microenvironment parameters of individual\ntryptophan residues","volume":"81","author":"Reshetnyak","year":"2001","journal-title":"Biophys. J."},{"key":"2026090112462969300_cit57","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/S0006-3495(00)76273-4","article-title":"The key event in force-induced\nunfolding of titin\u2019s\nimmunoglobulin domains","volume":"79","author":"Lu","year":"2000","journal-title":"Biophys. 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