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Titolo:
The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom
Autore:
Calvete, JJ; Moreno-Murciano, MP; Sanz, L; Jurgens, M; Schrader, M; Raida, M; Benjamin, DC; Fox, JW;
Indirizzi:
CSIC, Inst Biomed, E-46010 Valencia, Spain CSIC Valencia Spain E-46010CSIC, Inst Biomed, E-46010 Valencia, Spain BioVis GMBH & Co KG, D-30625 Hannover, Germany BioVis GMBH & Co KG Hannover Germany D-30625 , D-30625 Hannover, Germany Niedersachs Inst Peptid Forsch GMBH, D-30625 Hannover, Germany NiedersachsInst Peptid Forsch GMBH Hannover Germany D-30625 er, Germany Univ Virginia, Hlth Sci Ctr, Beirne B Carter Ctr Immunol Res, Charlottesville, VA 22908 USA Univ Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA Univ Virginia, Hlth Sci Ctr, Dept Microbiol, Charlottesville, VA 22908 USAUniv Virginia Charlottesville VA USA 22908 Charlottesville, VA 22908 USA
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 7, volume: 9, anno: 2000,
pagine: 1365 - 1373
SICI:
0961-8368(200007)9:7<1365:TDBPOC>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET-AGGREGATION INHIBITOR; NECROSIS-FACTOR-ALPHA; SPERM-EGG FUSION; BIOLOGICAL-ACTIVITY; FERTILIN-BETA; SNAKE-VENOMS; HEMORRHAGIC METALLOPROTEINASES; HETERODIMERIC DISINTEGRIN; MOLECULAR-CLONING; SEQUENCE-ANALYSIS;
Keywords:
ADAM; catrocollastatin-C; cysteine-rich domain; disintegrin-like domain; disulfide bond pattern; mass spectrometry; Reprolysin protein family; snake venom protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Calvete, JJ CSIC, Inst Biomed, Jaime Roig 11, E-46010 Valencia, Spain CSICJaime Roig 11 Valencia Spain E-46010 010 Valencia, Spain
Citazione:
J.J. Calvete et al., "The disulfide bond pattern of catrocollastatin C, a disintegrin-like/cysteine-rich protein isolated from Crotalus atrox venom", PROTEIN SCI, 9(7), 2000, pp. 1365-1373

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 thatis 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 fur ADAMs, PIII, and PII SVMPs based on disulfide bond engineering is also proposed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/06/20 alle ore 00:05:29