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Titolo:
Zooming in on the hydrophobic ridge of H-2D(b): Implications for the conformational variability of bound peptides
Autore:
Ciatto, C; Tissot, AC; Tschopp, M; Capitani, G; Pecorari, F; Pluckthun, A; Grutter, MG;
Indirizzi:
Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 chem, CH-8057 Zurich, Switzerland Cytos Biotechnol AG, CH-8952 Zurich, Switzerland Cytos Biotechnol AG Zurich Switzerland CH-8952 -8952 Zurich, Switzerland Univ Paris 11, Inst Biochim, UMR 8619, Lab Modelisat & Ingn Prot, F-91405 Orsay, France Univ Paris 11 Orsay France F-91405 at & Ingn Prot, F-91405 Orsay, France
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 5, volume: 312, anno: 2001,
pagine: 1059 - 1071
SICI:
0022-2836(20011005)312:5<1059:ZIOTHR>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR HISTOCOMPATIBILITY COMPLEX; T-CELL RECEPTOR; CLASS-I MOLECULES; 3-DIMENSIONAL STRUCTURE; CRYSTAL-STRUCTURE; LYMPHOCYTIC CHORIOMENINGITIS; CROSS-REACTIVITY; VIRAL PEPTIDES; MHC MOLECULES; BINDING;
Keywords:
major histocompatibility complex; T-cell receptors; antigen recognition; molecular evolution; crystal structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Grutter, MG Univ Zurich, Inst Biochem, Winterthurerstr 190, CH-8057 Zurich, Switzerland Univ Zurich Winterthurerstr 190 Zurich Switzerland CH-8057 nd
Citazione:
C. Ciatto et al., "Zooming in on the hydrophobic ridge of H-2D(b): Implications for the conformational variability of bound peptides", J MOL BIOL, 312(5), 2001, pp. 1059-1071

Abstract

Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cellreceptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 Angstrom and 2.20 Angstrom resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L-d-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 19:51:21