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An update on factor XI structure and function

DOI: 10.1016/j.thromres.2017.10.008 DOI Help

Authors: Bassem M. Mohammed (Vanderbilt University Medical Center; Cairo University) , Anton Matafonov (Vanderbilt University Medical Center) , Ivan Ivanov (Vanderbilt University Medical Center) , Mao-fu Sun (Vanderbilt University Medical Center) , Qiufang Cheng (Vanderbilt University Medical Center) , S. Kent Dickeson (Vanderbilt University Medical Center) , Chan Li (University of Nottingham) , David Sun (Vanderbilt University Medical Center) , Ingrid M. Verhamme (Vanderbilt University Medical Center) , Jonas Emsley (University of Nottingham) , David Gailani (Vanderbilt University Medical Center)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Thrombosis Research , VOL 161 , PAGES 94 - 105

State: Published (Approved)
Published: January 2018
Diamond Proposal Number(s): 14692

Open Access Open Access

Abstract: Factor XI (FXI) is the zymogen of a plasma protease, factor XIa (FXIa), that contributes to thrombin generation during blood coagulation by proteolytic activation of several coagulation factors, most notably factor IX (FIX). FXI is a homolog of prekallikrein (PK), a component of the plasma kallikrein-kinin system. While sharing structural and functional features with PK, FXI has undergone adaptive changes that allow it to contribute to blood coagulation. Here we review current understanding of the biology and enzymology of FXI, with an emphasis on structural features of the protein as they relate to protease function.

Subject Areas: Biology and Bio-materials, Medicine, Chemistry

Instruments: I02-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography