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Titolo:
Crystal structure of a T cell receptor V alpha 11 (AV11S5) domain: New canonical forms for the first and second complementarity determining regions
Autore:
Machius, M; Cianga, P; Deisenhofer, J; Ward, ES;
Indirizzi:
Univ Texas, SW Med Ctr, Ctr Immunol, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Med Ctr, Ctr Immunol, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Ctr Canc Immunobiol, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 Ctr Canc Immunobiol, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Howard Hughes Med Inst, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ward Hughes Med Inst, Dallas, TX 75390 USA Univ Texas, SW Med Ctr, Dept Biochem, Dallas, TX 75390 USA Univ Texas Dallas TX USA 75390 ed Ctr, Dept Biochem, Dallas, TX 75390 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 4, volume: 310, anno: 2001,
pagine: 689 - 698
SICI:
0022-2836(20010720)310:4<689:CSOATC>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
V-ALPHA DOMAIN; COLLAGEN-INDUCED ARTHRITIS; ELECTRON-DENSITY MAPS; MHC CLASS-II; PEPTIDE-MHC; ANTIGEN RECEPTOR; ANTAGONIST LIGANDS; MOLECULAR MIMICRY; 2.5 ANGSTROM; BETA DOMAIN;
Keywords:
T cell receptor V alpha domain; complementarity determining region; canonical form; X-ray crystallography; antigen recognition;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Ward, ES Univ Texas, SW Med Ctr, Ctr Immunol, 5323 Harry Hines Blvd, Dallas, TX 75390 USA Univ Texas 5323 Harry Hines Blvd Dallas TX USA 75390 TX 75390 USA
Citazione:
M. Machius et al., "Crystal structure of a T cell receptor V alpha 11 (AV11S5) domain: New canonical forms for the first and second complementarity determining regions", J MOL BIOL, 310(4), 2001, pp. 689-698

Abstract

We describe the X-ray crystallographic structure of a murine T cell receptor (TCR) V alpha domain ("V alpha 85.33 "; AV11S5-AJ17) to 1.85 Angstrom resolution. The V alpha 85.33 domain is derived from a TCR that recognizes a type II collagen peptide associated with the murine major histocompatibility complex (MHC) class II molecule, I-A(q). V alpha 85.33 packs as a V alpha-V alpha homodimer with a highly symmetric monomer-monomer interface. The first and second complementarity determining regions (CDR1 and CDR2) of this Ver are shorter than the CDRs corresponding to the majority of other V alpha gene families, and three-dimensional structures of CDRs of these lengths have not been described previously. The CDR1 and CDR2 therefore representnew canonical forms that could serve as templates for AV11 family members. CDR3 of the V alpha 85.33 domain is highly flexible and this is consistentwith plasticity of this region of the TCR. The fourth hypervariable loop (HV4 alpha) of AV11 and AV10 family members is one residue longer than that of other HV4 alpha regions and shows a high degree of flexibility. The increase in length results in a distinct disposition of the conserved residue Lys68, which has been shown in other studies to play a role in antigen recognition. The X-ray structure of V alpha 85.33 extends the database of canonical forms for CDR1 and CDR2, and has implications for antigen recognition by TCRs that contain related Vex domains. (C) 2001 Academic Press.

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Documento generato il 25/11/20 alle ore 10:25:43