1999
DOI: 10.1038/46594
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Crystal structures of the membrane-binding C2 domain of human coagulation factor V

Abstract: 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 wit… Show more

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Cited by 240 publications
(315 citation statements)
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References 26 publications
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“…Table 2 Absolute, E b , and relative, vE b , interaction energies in kcal/mol of the central residue X with the A-B part in the AXB complexes (see Section 2) ular level this analysis o¡ers a rationale for the observed misfunctioning of mutated retinoschisis, which seems to be correlated with the compromised stability of the WRW triad. Moreover the analysis of the surface of the RS1 model allowed us to identify an exposed hydrophobic patch, thus suggesting a possible role of RS1 in phospholipid membrane interaction, in a manner similar to what previously was proposed for FaV [10] and FaVIII [11,14].…”
Section: Discussionmentioning
confidence: 84%
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“…Table 2 Absolute, E b , and relative, vE b , interaction energies in kcal/mol of the central residue X with the A-B part in the AXB complexes (see Section 2) ular level this analysis o¡ers a rationale for the observed misfunctioning of mutated retinoschisis, which seems to be correlated with the compromised stability of the WRW triad. Moreover the analysis of the surface of the RS1 model allowed us to identify an exposed hydrophobic patch, thus suggesting a possible role of RS1 in phospholipid membrane interaction, in a manner similar to what previously was proposed for FaV [10] and FaVIII [11,14].…”
Section: Discussionmentioning
confidence: 84%
“…This patch is highly reminiscent of the hydrophobic surface around the spikes observed for both FaV (W26, W27, M83, L79) [10,33] and FaVIII (V2223, M2199, F2200, L2251, L2252) [11,34], which are likely candidates for phospholipid bilayer binding. Membrane involvement seems to be a com- mon feature for several members of the discoidin domain family.…”
Section: Resultsmentioning
confidence: 99%
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“…Three flexible loops protrude from the tip of the domain. In some cases, two of these loops form a pocket that mediates the binding of Ca 2 + and other divalent cations (Sutton and Sprang 1995; Sutton et al 1995, Sutton et al 1999; Grobler et al 1996; Perisic et al 1998; Ubach et al 1998a,Ubach et al 1998b; Pratt et al 1999; Macedo-Ribeiro et al 1999). Ca 2 + binding regulates the interaction of some C2 domains with target molecules including lipids and proteins, while other C2 domains do not appear to bind Ca 2 +.…”
Section: Introductionmentioning
confidence: 99%
“…Noncovalent FV-MMRN1 binding involves an extended region of the FV light chain C2 domain, that overlaps the FVa membrane binding site [4]. Recently solved FVa crystal structures and mutagenesis studies of FV function have provided evidence that the C domains of FV use structurally similar features to promote FVa binding to phospholipid membranes [5][6][7][8]. Nonetheless, the functions of the FV C1 domain are not as well characterized as those of the C2 domain.…”
mentioning
confidence: 99%