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

Manfred S. Weiss; Hubert J. Metzner; Rolf Hilgenfeld

doi:10.1016/S0014-5793(98)00098-2

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

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

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie

Leibniz-Institut für Altersforschung (Fritz Lipmann Institute)

144 Zitate (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.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	423
Ausgabenummer	3
Seiten (von - bis)	291-296
Seitenumfang	6
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(98)00098-2
Publikationsstatus	Veröffentlicht - 27.02.1998

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10.1016/S0014-5793(98)00098-2

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title = "Two non-proline cis peptide bonds may be important for factor XIII function",

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 {\AA} 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.",

author = "Weiss, \{Manfred S.\} and Metzner, \{Hubert J.\} and Rolf Hilgenfeld",

year = "1998",

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doi = "10.1016/S0014-5793(98)00098-2",

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T1 - Two non-proline cis peptide bonds may be important for factor XIII function

AU - Weiss, Manfred S.

AU - Metzner, Hubert J.

AU - Hilgenfeld, Rolf

PY - 1998/2/27

Y1 - 1998/2/27

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/18744421735

U2 - 10.1016/S0014-5793(98)00098-2

DO - 10.1016/S0014-5793(98)00098-2

M3 - Journal articles

C2 - 9515726

AN - SCOPUS:18744421735

SN - 0014-5793

VL - 423

SP - 291

EP - 296

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

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

Abstract

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