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Titolo:
CHLORAMINE T-INDUCED STRUCTURAL AND BIOCHEMICAL-CHANGES IN ECHISTATIN
Autore:
KUMAR CC; NIE HM; ARMSTRONG L; ZHANG RM; VIJAYKUMAR S; TSARBOPOULOS A;
Indirizzi:
SCHERING PLOUGH CORP,RES INST,DEPT TUMOR BIOL,2015 GALLOPING HILL RD KENILWORTH NJ 07033 TEMPLE UNIV,SCH MED,FELS INST CANC RES & MOL BIOL PHILADELPHIA PA 19140
Titolo Testata:
FEBS letters
fascicolo: 3, volume: 429, anno: 1998,
pagine: 239 - 248
SICI:
0014-5793(1998)429:3<239:CTSABI>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTEGRIN ALPHA(V)BETA(3); PLATELET-AGGREGATION; SIGNAL-TRANSDUCTION; MASS-SPECTROMETRY; CELL-ADHESION; RGD PROTEIN; DISINTEGRINS; ANTAGONISTS; INHIBITOR; CARINATUS;
Keywords:
ECHISTATIN; INTEGRIN RECEPTOR; CHLORAMINE T; OXIDATION; RGD MOTIF;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
C.C. Kumar et al., "CHLORAMINE T-INDUCED STRUCTURAL AND BIOCHEMICAL-CHANGES IN ECHISTATIN", FEBS letters, 429(3), 1998, pp. 239-248

Abstract

Echistatin is a member of the disintegrin family of peptides and a potent inhibitor of platelet aggregation and cell adhesion. Echistatin binds to integrin alpha(v)beta(3) and alpha(IIb)beta(3) receptors with high affinity. Binding is mediated by an RGD-containing loop maintained in an appropriate conformation by disulfide bridges, In this study, we hale compared the binding characteristics of echistatin iodinated by either lactoperoxidase or chloramine T method, We show that echistatin labeled by lactoperoxidase method binds to integrin alpha(v)beta(3)receptor with high affinity and in a non-dissociable manner very similar to native echistatin, In contrast, chloramine T-labeled echistatincan rapidly dissociate from the receptor. We demonstrate that chloramine T reaction results in the addition of an extra oxygen to the methionine residue adjacent to the RGD motif in echistatin. Modeling studies and molecular dynamic simulation studies show that the extra oxygen atom on the methionine residue can form hydrogen bonds with the glycine and aspartic acid residues of the RGD motif, These structural changes in echistatin help explain the changes in the binding characteristics of the molecule following chloramine T reaction. (C) 1998 Federationof European Biochemical Societies.

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Documento generato il 04/12/20 alle ore 19:51:54