Structure and function studies of factor XIIIa by x-ray crystallography.

Abstract:

:The three-dimensional structures of several forms of the factor XIII A subunit have been determined using single crystal x-ray diffraction methods. Our crystallographic studies have provided the first detailed structural view of the factor XIII A subunit and information that is useful for understanding transglutaminase function. We have identified a conserved Cys314-His373-Asp396 catalytic triad of residues in the active site of the molecule and a number of other conserved residues that may play important roles as well. The calcium and strontium structures have revealed several conserved acidic residues (Asp438, Glu485, and Glu490) involved in ion binding. We have also been able to use our crystal structures as scaffolds to model the possible structural effects of missense mutations that have been identified in factor XIII-deficient patients.

journal_name

Semin Thromb Hemost

authors

Yee VC,Le Trong I,Bishop PD,Pedersen LC,Stenkamp RE,Teller DC

doi

10.1055/s-2007-999035

subject

Has Abstract

pub_date

1996-01-01 00:00:00

pages

377-84

issue

5

eissn

0094-6176

issn

1098-9064

journal_volume

22

pub_type

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