Interaction of factor V B-domain acidic region with its basic region and with TFPI/TFPI2: Structural insights from molecular modeling studies.

ABSTRACT: Factor V (FV) B-domain contains an acidic region (FV-AR2) and a basic region (FV-BR), which interact with each other and maintain FV in a procofactor form; removal of either region via deletion/proteolysis results in an active FVa molecule. Tissue factor pathway inhibitor type-1 (TFPI) and type-2 (TFPI2) each contain a C-terminus basic segment homologous to FV-BR; this region in TFPI (and predicted in TFPI2) binds to FV-AR2 in platelet FVa (that lacks FV-BR) with high affinity and inhibits FVa function. To understand molecular interactions between FV-AR2 with FV-BR, TFPI-BR and TFPI2-BR. Circular dichroism (CD) and molecular modeling approaches. CD experiments reveal the presence of ∼20% helical content in both FV-AR2 and FV-BR but each lacks beta-sheet. Predicted structures of FV-AR2 and

SUBMITTER: Vadivel K 

PROVIDER: S-EPMC5568831 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature