Identification of the Calcium Binding Site and a Novel Ytterbium Site in Blood Coagulation Factor XIII by X-ray Crystallography
The presence or absence of calcium determines the activation, activity, oligomerization, and stability of blood coagulation factor XIII. To explore these observed effects, we have determined the x-ray crystal structure of recombinant factor XIII A 2 in the presence of calcium, strontium, and ytterbi...
Gespeichert in:
Veröffentlicht in: | The Journal of biological chemistry 1999-02, Vol.274 (8), p.4917-4923 |
---|---|
Hauptverfasser: | , , , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
Zusammenfassung: | The presence or absence of calcium determines the activation, activity, oligomerization, and stability of blood coagulation
factor XIII. To explore these observed effects, we have determined the x-ray crystal structure of recombinant factor XIII
A 2 in the presence of calcium, strontium, and ytterbium. The main calcium binding site within each monomer involves the main
chain oxygen atom of Ala-457, and also the side chains from residues Asn-436, Asp-438, Glu-485, and Glu-490. Calcium and strontium
bind in the same location, while ytterbium binds several angstroms removed. A novel ytterbium binding site is also found at
the dimer two-fold axis, near residues Asp-270 and Glu-272, and this site may be related to the reported inhibition by lanthanide
metals (Achyuthan, K. E., Mary, A., and Greenberg, C. S. (1989) Biochem. J. 257, 331â338). The overall structure of ion-bound factor XIII is very similar to the previously determined crystal structures
of factor XIII zymogen, likely due to the constraints of this monoclinic crystal form. We have merged the three independent
sets of water molecules in the structures to determine which water molecules are conserved and possibly structurally significant. |
---|---|
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1074/jbc.274.8.4917 |