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Two non‐proline cis peptide bonds may be important for factor XIII function
Author(s) -
Weiss Manfred S,
Metzner Hubert J,
Hilgenfeld Rolf
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00098-2
Subject(s) - zymogen , chemistry , peptide , cysteine , proline , peptide bond , stereochemistry , residue (chemistry) , peptide conformation , biochemistry , amino acid , enzyme
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 Arg 310 and Tyr 311 close to the active site cysteine residue (Cys 314 ) and the other is between Gln 425 and Phe 426 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.