| pubmed-article:10586886 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10586886 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:10586886 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:10586886 | lifeskim:mentions | umls-concept:C0015498 | lld:lifeskim |
| pubmed-article:10586886 | lifeskim:mentions | umls-concept:C1511359 | lld:lifeskim |
| pubmed-article:10586886 | pubmed:issue | 6760 | lld:pubmed |
| pubmed-article:10586886 | pubmed:dateCreated | 1999-12-10 | lld:pubmed |
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| pubmed-article:10586886 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:abstractText | Rapid and controlled clot formation is achieved through sequential activation of circulating serine proteinase precursors on phosphatidylserine-rich procoagulant membranes of activated platelets and endothelial cells. The homologous complexes Xase and prothrombinase, each consisting of an active proteinase and a non-enzymatic cofactor, perform critical steps within this coagulation cascade. The activated cofactors VIIIa and Va, highly specific for their cognate proteinases, are each derived from precursors with the same A1-A2-B-A3-C1-C2 architecture. Membrane binding is mediated by the C2 domains of both cofactors. Here we report two crystal structures of the C2 domain of human factor Va. The conserved beta-barrel framework provides a scaffold for three protruding loops, one of which adopts markedly different conformations in the two crystal forms. We propose a mechanism of calcium-independent, stereospecific binding of factors Va and VIIIa to phospholipid membranes, on the basis of (1) immersion of hydrophobic residues at the apices of these loops in the apolar membrane core; (2) specific interactions with phosphatidylserine head groups in the groove enclosed by these loops; and (3) favourable electrostatic contacts of basic side chains with negatively charged membrane phosphate groups. | lld:pubmed |
| pubmed-article:10586886 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10586886 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10586886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10586886 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10586886 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:10586886 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:BodeWW | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:HuberRR | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:KaneW HWH | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:KimS WSW | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:OrtelT LTL | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:Quinn-AllenM... | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:BartunikH DHD | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:StubbsM TMT | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:Macedo-Ribeir... | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:BourenkovG... | lld:pubmed |
| pubmed-article:10586886 | pubmed:author | pubmed-author:Fuentes-Prior... | lld:pubmed |
| pubmed-article:10586886 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10586886 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:10586886 | pubmed:volume | 402 | lld:pubmed |
| pubmed-article:10586886 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10586886 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10586886 | pubmed:pagination | 434-9 | lld:pubmed |
| pubmed-article:10586886 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10586886 | pubmed:meshHeading | pubmed-meshheading:10586886... | lld:pubmed |
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| pubmed-article:10586886 | pubmed:meshHeading | pubmed-meshheading:10586886... | lld:pubmed |
| pubmed-article:10586886 | pubmed:meshHeading | pubmed-meshheading:10586886... | lld:pubmed |
| pubmed-article:10586886 | pubmed:meshHeading | pubmed-meshheading:10586886... | lld:pubmed |
| pubmed-article:10586886 | pubmed:meshHeading | pubmed-meshheading:10586886... | lld:pubmed |
| pubmed-article:10586886 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10586886 | pubmed:articleTitle | Crystal structures of the membrane-binding C2 domain of human coagulation factor V. | lld:pubmed |
| pubmed-article:10586886 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Martinsried, Germany. | lld:pubmed |
| pubmed-article:10586886 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10586886 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:10586886 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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