pubmed-article:15014436 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0006675 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0076560 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C1708096 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C1705914 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
pubmed-article:15014436 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
pubmed-article:15014436 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:15014436 | pubmed:dateCreated | 2004-3-24 | lld:pubmed |
pubmed-article:15014436 | pubmed:abstractText | Thrombospondins (TSPs) are extracellular regulators of cell-matrix interactions and cell phenotype. The most highly conserved region of all TSPs are the calcium-binding type 3 (T3) repeats and the C-terminal globular domain (CTD). The crystal structure of a cell-binding TSP-1 fragment, spanning three T3 repeats and the CTD, reveals a compact assembly. The T3 repeats lack secondary structure and are organised around a core of calcium ions; two DxDxDGxxDxxD motifs per repeat each encapsulate two calcium ions in a novel arrangement. The CTD forms a lectin-like beta-sandwich and contains four strictly conserved calcium-binding sites. Disruption of the hairpin structure of T3 repeats 6 and 7 decreases protein secretion and stability. The availability for cell attachment of an RGD motif in T3 repeat 7 is modulated by calcium loading. The central architectural role of calcium explains how it is critical for the functions of the TSP C-terminal region. Mutations in the T3 repeats of TSP-5/COMP, which cause two human skeletal disorders, are predicted to disrupt the tertiary structure of the T3-CTD assembly. | lld:pubmed |
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pubmed-article:15014436 | pubmed:language | eng | lld:pubmed |
pubmed-article:15014436 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15014436 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15014436 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:15014436 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15014436 | pubmed:month | Mar | lld:pubmed |
pubmed-article:15014436 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:15014436 | pubmed:author | pubmed-author:KvansakulMarc... | lld:pubmed |
pubmed-article:15014436 | pubmed:author | pubmed-author:HohenesterErh... | lld:pubmed |
pubmed-article:15014436 | pubmed:author | pubmed-author:AdamsJosephin... | lld:pubmed |
pubmed-article:15014436 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15014436 | pubmed:day | 24 | lld:pubmed |
pubmed-article:15014436 | pubmed:volume | 23 | lld:pubmed |
pubmed-article:15014436 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15014436 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15014436 | pubmed:pagination | 1223-33 | lld:pubmed |
pubmed-article:15014436 | pubmed:dateRevised | 2010-4-26 | lld:pubmed |
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