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Titolo:
Crystal structure of an isolated V-alpha domain of the 2C T-cell receptor
Autore:
Rudolph, MG; Huang, MD; Teyton, L; Wilson, IA;
Indirizzi:
Scripps Res Inst, Inst Chem Biol, Dept Mol Biol & Skaggs, La Jolla, CA 92037 USA Scripps Res Inst La Jolla CA USA 92037 l & Skaggs, La Jolla, CA 92037 USA Scripps Res Inst, Dept Immunol, La Jolla, CA 92037 USA Scripps Res Inst La Jolla CA USA 92037 pt Immunol, La Jolla, CA 92037 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 314, anno: 2001,
pagine: 1 - 8
SICI:
0022-2836(20011116)314:1<1:CSOAIV>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONOCLONAL-ANTIBODY THERAPY; SYSTEMIC VASCULITIS; PROTEIN STRUCTURES; ANTIGEN RECEPTOR; 2.5 ANGSTROM; BETA-CHAIN; AFFINITY; PEPTIDE; COMPLEX; ERRORS;
Keywords:
T-cell receptor variable domain; complementarity-determining regions; antibody engineering; protein crystallization; immunoglobulin fold;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
54
Recensione:
Indirizzi per estratti:
Indirizzo: Wilson, IA Scripps Res Inst, Inst Chem Biol, Dept Mol Biol & Skaggs, 10550N Torrey,Pines Rd,BBC 206, La Jolla, CA 92037 USA Scripps Res Inst 10550 NTorrey,Pines Rd,BBC 206 La Jolla CA USA 92037
Citazione:
M.G. Rudolph et al., "Crystal structure of an isolated V-alpha domain of the 2C T-cell receptor", J MOL BIOL, 314(1), 2001, pp. 1-8

Abstract

The T-cell receptor (TCR) is a heterodimeric cell-surface protein consisting of two chains, alpha and beta, each of which is composed of a variable (V) and a constant (C) domain. Crystals of the isolated V-alpha domain of the murine TCR 2C were grown by serendipity from a solution containing the extracellular domains of the intact TCR 2C and CD3 gamma epsilon -chains. TheV-alpha crystal structure shows how crystal packing can substitute for another V-alpha domain in a different fashion from that observed in V-alpha/V-beta homodimer and V-alpha/V-beta heterodimer structures. Significant conformational changes occur in the CDR3 and beta (3)beta (4) loops that normally form part of the dimer interface. The monomeric V-alpha domain provides the unique opportunity to study the effect of dimerization on the conformation of the unliganded complementarity-determining regions (CDR) of a TCR. This structure of an individual V-alpha module has implications for stabilityand bioengineering of isolated antibody and immunoglobulin domains. (C) 2001 Academic Press.

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Documento generato il 29/09/20 alle ore 10:33:16