9D5D

Crystal Structure of Blood Coagulation Factor VIII C2 Domain Mutant L2251A/L2252A

This is a non-PDB format compatible entry.

Summary for 9D5D

• Entry DOI: 10.2210/pdb9d5d/pdb
• Descriptor: Factor VIIIa light chain (2 entities in total)
• Functional Keywords: blood coagulation factor viii, lipid binding protein, factor viii c2 domain mutant, blood clotting
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18563.10

Authors

Avery, N.G.,Childers, K.C.,Spiegel, P.C. (deposition date: 2024-08-13, release date: 2024-09-04, Last modification date: 2024-12-18)

Primary citation

Avery, N.G.,Young, I.R.,Lu, S.,Vaughan, J.D.,Korus, P.S.,Richardson, T.N.,Childers, K.C.,Smirnov, S.L.,Spiegel Jr., P.C.
Biophysical characterization of blood coagulation factor VIII binding to lipid nanodiscs that mimic activated platelet surfaces.
J.Thromb.Haemost., 2024

PubMed Abstract: Following proteolytic activation, activated blood coagulation factor (F)VIII (FVIIIa) binds to activated platelet membranes, forming the intrinsic tenase complex with activated FIX (FIXa). Previous studies have identified the C1 and C2 domains as the membrane binding domains of FVIII through conserved arginine residues. A membrane binding model for the FVIII C domains proposes that surface-exposed hydrophobic and positively charged residues at each C domain interact with the membrane, yet a comprehensive thermodynamic and structural description of this interaction is lacking.

PubMed: 39549835
DOI: 10.1016/j.jtha.2024.11.003

Experimental method

X-RAY DIFFRACTION (1.83 Å)