3S9C

Russell's viper venom serine proteinase, RVV-V in complex with the fragment (residues 1533-1546) of human factor V

Summary for 3S9C

• Entry DOI: 10.2210/pdb3s9c/pdb
• Related: 3S9A 3S9B 3SBK
• Descriptor: Vipera russelli proteinase RVV-V gamma, Coagulation factor V, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: serine proteinase, double six-stranded beta-barrels, hydrolase, glycosylation
• Biological source: Daboia russellii siamensis (Siamese Russell's viper); More
• Total number of polymer chains: 2
• Total formula weight: 29006.03

Authors

Nakayama, D.,Ben Ammar, Y.,Takeda, S. (deposition date: 2011-06-01, release date: 2011-09-07, Last modification date: 2024-10-09)

Primary citation

Nakayama, D.,Ben Ammar, Y.,Miyata, T.,Takeda, S.
Structural basis of coagulation factor V recognition for cleavage by RVV-V
Febs Lett., 585:3020-3025, 2011

PubMed Abstract: Russell's viper venom factor V (FV) activator (RVV-V) is a thrombin-like proteinase that specifically cleaves the Arg1545-Ser1546 bond of FV. Here we present the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8Å resolution. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P(7))-Arg1545 (P(1)), of the cleaved substrate. Comparison with substrate-free structures reveals conformational changes of the RVV-V loops upon substrate binding, suggesting that the multiple interactions are mediated by an induced-fit mechanism. The results provide an explanation for the narrow specificity of RVV-V.

PubMed: 21871889
DOI: 10.1016/j.febslet.2011.08.022

Experimental method

X-RAY DIFFRACTION (1.8 Å)