{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T07:53:32Z","timestamp":1791186812923,"version":"4.1.0"},"reference-count":38,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2013,11,25]],"date-time":"2013-11-25T00:00:00Z","timestamp":1385337600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100011781","name":"Shriners Hospital for Children","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100011781","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2014,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The FK506\u2010binding protein (FKBP) family consists of proteins with a variety of protein\u2013protein interaction domains and versatile cellular functions. It is assumed that all members are peptidyl\u2010prolyl <jats:italic>cis\u2013trans<\/jats:italic> isomerases with the enzymatic function attributed to the FKBP domain. Six members of this family localize to the mammalian endoplasmic reticulum (ER). Four of them, FKBP22 (encoded by the <jats:italic>FKBP14<\/jats:italic> gene), FKBP23 (<jats:italic>FKBP7<\/jats:italic>), FKBP60 (<jats:italic>FKBP9<\/jats:italic>), and FKBP65 (<jats:italic>FKBP10<\/jats:italic>), are unique among all FKBPs as they contain the EF\u2010hand motifs. Little is known about the biological roles of these proteins, but emerging genetics studies are attracting great interest to the ER resident FKBPs, as mutations in genes encoding <jats:italic>FKBP10<\/jats:italic> and <jats:italic>FKBP14<\/jats:italic> were shown to cause a variety of matrix disorders. Although the structural organization of the FKBP\u2010type domain as well as of the EF\u2010hand motif has been known for a while, it is difficult to conclude how these structures are combined and how it affects the protein functionality. We have determined a unique 1.9 \u00c5 resolution crystal structure for human FKBP22, which can serve as a prototype for other EF hand\u2010containing FKBPs. The EF\u2010hand motifs of two FKBP22 molecules form a dimeric complex with an elongated and predominantly hydrophobic cavity that can potentially be occupied by an aliphatic ligand. The FKBP\u2010type domains are separated by a cleft and their putative active sites can catalyze isomerazation of two bonds within a polypeptide chain in extended conformation. These structural results are of prime interest for understanding biological functions of ER resident FKBPs containing EF\u2010hand motifs.<\/jats:p>","DOI":"10.1002\/pro.2391","type":"journal-article","created":{"date-parts":[[2013,10,29]],"date-time":"2013-10-29T11:08:38Z","timestamp":1383044918000},"page":"67-75","source":"Crossref","is-referenced-by-count":27,"title":["Structure of human peptidyl\u2010prolyl <i>cis\u2013trans<\/i> isomerase FKBP22 containing two EF\u2010hand motifs"],"prefix":"10.1002","volume":"23","author":[{"given":"Sergei P.","family":"Boudko","sequence":"first","affiliation":[{"name":"Research Department Shriners Hospital for Children Portland Oregon 97239"},{"name":"Department of Biochemistry and Molecular Biology Oregon Health and Science University Portland Oregon 97239"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yoshihiro","family":"Ishikawa","sequence":"additional","affiliation":[{"name":"Research Department Shriners Hospital for Children Portland Oregon 97239"},{"name":"Department of Biochemistry and Molecular Biology Oregon Health and Science University Portland Oregon 97239"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jay","family":"Nix","sequence":"additional","affiliation":[{"name":"Molecular Biology Consortium Advanced Light Source Beamline, Lawrence Berkeley National Laboratory Berkeley California 94720"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael S.","family":"Chapman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biology Oregon Health and Science University Portland Oregon 97239"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hans Peter","family":"B\u00e4chinger","sequence":"additional","affiliation":[{"name":"Research Department Shriners Hospital for Children Portland Oregon 97239"},{"name":"Department of Biochemistry and Molecular Biology Oregon Health and Science University Portland Oregon 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