Literature summary for 3.4.21.95 extracted from

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

Search for more literature for 3.4.21.95

Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8 A resolution is shown. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P7)-Arg1545 (P1), 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	Daboia russelii

Crystallization (Comment)

Organism

the crystal structure of RVV-V in complex with the FV14 peptide (residues 1533-1546 of human FV) determined at 1.8 A resolution is shown. The structure reveals multiple interactions between RVV-V and the seven residues, Ile1539 (P7)-Arg1545 (P1), 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

Daboia russelii

Organism

Organism	UniProt	Comment	Textmining
Daboia russelii	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Ac-SRDPDNIAAWYLRS + H2O	synthetic N-acetylated 14-amino acid peptide (FV-14)	Daboia russelii	?	-	?

Synonyms

Synonyms	Comment	Organism
Russell's viper venom factor V (FV) activator	-	Daboia russelii
RVV-V	-	Daboia russelii

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Release 2023.1 (January 2023)