Two non‐proline cis peptide bonds may be important for factor XIII function

FEBS Letters

Weiss, Manfred S¹  Metzner, Hubert J²  Hilgenfeld, Rolf¹ 

[1] Institute of Molecular Biotechnology, Department of Structural Biology and Crystallography, P.O. Box 100813, D-07708 Jena, Germany;Centeon Pharma GmbH, P.O. Box 1240, D-35002 Marburg, Germany

关键词: Protein structure;    Blood coagulation;    Transglutaminase;    cis Peptide;    Factor XIII activation;   

DOI  :  10.1016/S0014-5793(98)00098-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic crystal form and refined to an R-factor of 18.3% (R _free=23.6%) for all data between 40.0 and 2.1 Å resolution. Two non-proline cis peptide bonds were detected. One is between Arg³¹⁰ and Tyr³¹¹ close to the active site cysteine residue (Cys³¹⁴) and the other is between Gln⁴²⁵ and Phe⁴²⁶ at the dimerization interface. The structure and the role of these cis peptides are discussed in the light of their possible importance for factor XIII function.

【 授权许可】

Unknown