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

Manfred S. Weiss, Hubert J. Metzner, Rolf Hilgenfeld*

*Corresponding author for this work
133 Citations (Scopus)

Abstract

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 Gin425 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.

Original languageEnglish
JournalFEBS Letters
Volume423
Issue number3
Pages (from-to)291-296
Number of pages6
ISSN0014-5793
DOIs
Publication statusPublished - 27.02.1998

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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