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Titolo:
Structure of a human gamma delta T-cell antigen receptor
Autore:
Allison, TJ; Winter, CC; Fournie, JJ; Bonneville, M; Garboczi, DN;
Indirizzi:
NIAID, Struct Biol Sect, Immunogenet Lab, Rockville, MD 20852 USA NIAID Rockville MD USA 20852 ct, Immunogenet Lab, Rockville, MD 20852 USA CHU Purpan, INSERM, U395, F-31024 Toulouse, France CHU Purpan Toulouse France F-31024 NSERM, U395, F-31024 Toulouse, France Inst Biol, INSERM, U463, F-44035 Nantes, France Inst Biol Nantes France F-44035 ol, INSERM, U463, F-44035 Nantes, France
Titolo Testata:
NATURE
fascicolo: 6839, volume: 411, anno: 2001,
pagine: 820 - 824
SICI:
0028-0836(20010614)411:6839<820:SOAHGD>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
NONPEPTIDIC MYCOBACTERIAL LIGANDS; RECOGNITION; STIMULATION; CRYSTALLOGRAPHY; PYROPHOSPHATE; SUBSET; SUITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Allison, TJ NIAID, Struct Biol Sect, Immunogenet Lab, 12441 Parklawn Dr, Rockville, MD20852 USA NIAID 12441 Parklawn Dr Rockville MD USA 20852 le, MD20852 USA
Citazione:
T.J. Allison et al., "Structure of a human gamma delta T-cell antigen receptor", NATURE, 411(6839), 2001, pp. 820-824

Abstract

T-cell antigen receptors composed of gamma and delta polypeptide chains (gamma delta TCRs) can directly recognize antigens in the form of intact proteins or non-peptide compounds, unlike alpha beta TCRs, which recognize antigens bound to major histocompatibility complex molecules (MHC). About 5% ofperipheral blood T cells bear gamma delta TCRs, most of which recognize non-peptide phosphorylated antigens(1,2). Here we describe the 3.1 Angstrom resolution structure of a human gamma delta TCR from a T-cell clone(3) that is phosphoantigen-reactive. The orientation of the variable (V) and constant (C) regions of the gamma delta TCR is unique when compared with alpha beta TCRs or antibodies, and results from an unusually small angle between theV gamma and C gamma domains. The complementarity-determining regions (CDRs) of the V domains exhibit a chemically reasonable binding site for phosphorylated antigens, providing a possible explanation for the canonical usage of the V gamma9 and V delta2 gene segments by phosphoantigen-reactive receptors. Although the gamma delta TCR V domains are similar in overall structure to those of alpha beta TCRs, gamma delta TCR C domains are markedly different. Structural differences in C gamma and C delta, and in the location of the disulphide bond between them, may enable gamma delta TCRs to form different recognition/signalling complexes than alpha beta TCRs.

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Documento generato il 06/04/20 alle ore 05:05:46