Structure-function of anticoagulant TIX-5, the inhibitor of factor Xa-mediated FV activation.

ABSTRACT:

Background

The prothrombinase complex consists of factors Xa (FXa) and Va (FVa) on an anionic phospholipid surface and converts prothrombin into thrombin. Both coagulation factors require activation before complex assembly. We recently identified TIX-5, a unique anticoagulant tick protein that specifically inhibits FXa-mediated activation of FV. Because TIX-5 inhibited thrombin generation in blood plasma, it was concluded that FV activation by FXa contributes importantly to coagulation.

Objective

We aimed to unravel the structure-function relationships of TIX-5.

Method

We used a structure model generated based on homology with the allergen Der F7.

Results

Tick inhibitor of factor Xa toward FV was predicted to consist of a single rod formed by several beta sheet

SUBMITTER: Maag A 

PROVIDER: S-EPMC8360041 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature