PDB ID or protein name

1sdd » C2 domains of coagulation factor Va

1sdd » C2 domains of coagulation factor Va
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Topology in Eukaryotic plasma membrane
Topologyextracellular side
cytoplasmic side
1sdd » C2 domains of coagulation factor Va
Depth 3.7 ± 2.0 Å
Tilt Angle 35 ± 8°
ΔGtransfer -8.7 kcal/mol
Links to 1sdd PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology extracellular
Resolution 2.8 Å
Other PDB entries representing this structure none
Number of subunits 2
Experimental Verification for 1sdd » C2 domains of coagulation factor Va
Residues Y1956, L1957, W2063 and W2064 are involved in hydrophobic interactions with the membrane (Peng et al. 2004, 2005) in agreement with the set of calculated membrane core embedded residues Y1956, L1957, W2063 and W2064. Maximal membrane binding affinity is -9 kcal/mol (Koppaka and Lentz 1996) or -13 kcal/mol (Peng et al. 2004).
3 references
Koppaka, V., and Lentz, B.R. 1996. Binding of bovine factor Va to phosphatidylcholine membranes. Biophys. J. 70:2930-2937. PubMed
Peng W, Quinn-Allen MA, Kim SW, Alexander KA, Kane WH. 2004. Trp2063 and Trp2064 in the factor Va C2 domain are required for high-affinity binding to phospholipid membranes but not for assembly of the prothrombinase complex. Biochemistry. 43: 4385-4393. PubMed
Peng, W., Quinn-Allen, M.A., and Kane, W.H. 2005. Mutation of hydrophobic residues in the factor Va C1 and C2 domains blocks membrane-dependent prothrombin activation. J. Thromb. Haemost. 3:351-354. PubMed
Comments on 1sdd » C2 domains of coagulation factor Va
Coagulation factor V is a cofactor that participates with factor Xa to activate prothrombin to thrombin. Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). Factor Va is composed of a heavy chain and a light chain, noncovalently bound. The interaction between the two chains is calcium-dependent.