{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T23:12:04Z","timestamp":1790982724923,"version":"4.1.0"},"reference-count":57,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2009,3,10]],"date-time":"2009-03-10T00:00:00Z","timestamp":1236643200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["HL49081"],"award-info":[{"award-number":["HL49081"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["faseb.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FASEB Journal"],"published-print":{"date-parts":[[2009,8]]},"abstract":"<jats:p>\n                    Cartilage oligomeric matrix protein (COMP), or thrombospondin\u20105 (TSP\u20105), is a secreted glycoprotein that is important for growth plate organization and function. Mutations in COMP cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1). In this study, we determined the structure of a recombinant protein that contains the last epidermal growth factor repeat, the type 3 repeats and the C\u2010terminal domain (CTD) of COMP to 3.15\u2010\u00c4 resolution limit by X\u2010ray crystallography. The CTD is a \u03b2\u2010sandwich that is composed of 15 antiparallel P\u2010strands, and the type 3 repeats are a contiguous series of calcium binding sites that associate with the CTD at multiple points. The crystal packing reveals an exposed potential metal\u2010ion\u2010 dependent adhesion site (MIDAS) on one edge of the P\u2010sandwich that is common to all TSPs and may serve as a binding site for collagens and other ligands. Disease\u2010 causing mutations in COMP disrupt calcium binding, disulfide bond formation, intramolecular interactions, or sites for potential ligand binding. The structure presented here and its unique molecular packing in the crystal identify potential interactive sites for glycosaminoglycans, integrins, and collagens, which are key to cartilage structure and function.\u2014 Tan, K.,Duquette, M., Joachimiak, A., Lawler, J. The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.\n                    <jats:italic>FASEB J.<\/jats:italic>\n                    23, 2490\u20132501 (2009)\n                  <\/jats:p>","DOI":"10.1096\/fj.08-128090","type":"journal-article","created":{"date-parts":[[2009,3,10]],"date-time":"2009-03-10T21:47:55Z","timestamp":1236721675000},"page":"2490-2501","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":71,"title":["The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding"],"prefix":"10.1096","volume":"23","author":[{"given":"Kemin","family":"Tan","sequence":"first","affiliation":[{"name":"Biosciences Division The Midwest Center for Structural Genomics and Structural Biology Center Argonne National Laboratory Argonne Illinois"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark","family":"Duquette","sequence":"additional","affiliation":[{"name":"The Division of Cancer Biology and Angiogenesis Department of Pathology Beth Israel Deaconess Medical Center Boston Massachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrzej","family":"Joachimiak","sequence":"additional","affiliation":[{"name":"Biosciences Division The Midwest Center for Structural Genomics and Structural Biology Center Argonne National Laboratory Argonne Illinois"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jack","family":"Lawler","sequence":"additional","affiliation":[{"name":"The Division of Cancer Biology and Angiogenesis Department of Pathology Beth Israel Deaconess Medical Center Boston Massachusetts"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,3,10]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M504778200"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1063-4584(03)00055-4"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M608744200"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1128\/MCB.25.23.10465-10478.2005"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M611390200"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0945-053X(02)00015-X"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M705735200"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M403778200"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M009512200"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1002\/humu.10066"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.matbio.2004.09.006"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M009507200"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.32.20397"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80622-4"},{"key":"e_1_2_6_16_1","first-page":"101","article-title":"The mechanosensitivity of cartilage oligomeric matrix protein (COMP)","volume":"40","author":"Giannoni P.","year":"2003","journal-title":"Biorheology"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1172\/JCI0214386"},{"key":"e_1_2_6_18_1","doi-asserted-by":"publisher","DOI":"10.2353\/ajpath.2008.071094"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1002\/ajmg.1320450420"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1038\/nsmb997"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7600166"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444906019949"},{"key":"e_1_2_6_23_1","first-page":"905","article-title":"Crystallography & NMR system: A new software suite for macromolecular structure determination","volume":"54","author":"Br\u00e8unger A. 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