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The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom

Published online by Cambridge University Press:  01 July 2000

JUAN J. CALVETE ,
M. PAZ MORENO-MURCIANO ,
LIBIA SANZ ,
MICHAEL JÜRGENS ,
MICHAEL SCHRADER ,
MANFRED RAIDA ,
DAVID C. BENJAMIN  and
JAY W. FOX
JUAN J. CALVETE
Affiliation:
Instituto de Biomedicina, C.S.I.C., Jaime Roig 11, E-46010 Valencia, Spain
M. PAZ MORENO-MURCIANO
Affiliation:
Instituto de Biomedicina, C.S.I.C., Jaime Roig 11, E-46010 Valencia, Spain
LIBIA SANZ
Affiliation:
Instituto de Biomedicina, C.S.I.C., Jaime Roig 11, E-46010 Valencia, Spain
MICHAEL JÜRGENS
Affiliation:
BioVisioN GmbH & Co. KG, Feodor-Lynen-Strasse 5, D-30625 Hannover, Germany
MICHAEL SCHRADER
Affiliation:
BioVisioN GmbH & Co. KG, Feodor-Lynen-Strasse 5, D-30625 Hannover, Germany
MANFRED RAIDA
Affiliation:
Niedersächsisches Institut für Peptid-Forschung GmbH, Feodor-Lynen-Strasse 31, D-30625 Hannover, Germany
DAVID C. BENJAMIN
Affiliation:
Beirne B. Carter Center for Immunology Research, University of Virginia Health Sciences Center, MR4 Box 4012, Charlottesville, Virginia 22908
JAY W. FOX
Affiliation:
Department of Microbiology, University of Virginia Health Sciences Center, Box 441 Jordan Hall, Charlottesville, Virginia 22908
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Abstract

The disulfide bond pattern of catrocollastatin-C was determined by N-terminal sequencing and mass spectrometry. The N-terminal disintegrin-like domain is a compact structure including eight disulfide bonds, seven of them in the same pattern as the disintegrin bitistatin. The protein has two extra cysteine residues (XIII and XVI) that form an additional disulfide bond that is characteristically found in the disintegrin-like domains of cellular metalloproteinases (ADAMs) and PIII snake venom Zn-metalloproteinases (SVMPs). The C-terminal cysteine-rich domain of catrocollastatin-C contains five disulfide bonds between nearest-neighbor cysteines and a long range disulfide bridge between CysV and CysX. These results provide structural evidence for a redefinition of the disintegrin-like and cysteine-rich domain boundaries. An evolutionary pathway for ADAMs, PIII, and PII SVMPs based on disulfide bond engineering is also proposed.

Keywords

ADAMcatrocollastatin-Ccysteine-rich domaindisintegrin-like domaindisulfide bond patternmass spectrometryReprolysin protein familysnake venom protein
Type
Research Article
Information
Protein Science , Volume 9 , Issue 7 , July 2000 , pp. 1365 - 1373
Copyright
2000 The Protein Society

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