Structural highlights
Function
[HA11_MOUSE] Involved in the presentation of foreign antigens to the immune system. [B2MG_MOUSE] Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The decameric peptide SALQNAASIA from the Mycobacterium bovis heat shock protein (hsp) 60 is recognized by the murine T-cell receptor UZ-3-4 in complex with the murine class I major histocompatibility complex molecule H-2D(b). This T-cell receptor cross-reacts with the H-2D(b)-bound non-homologous decameric peptide KDIGNIISDA from the murine hsp60, but does not recognize the nonameric mycobacterial peptide SALQNAASI. Cross-recognition of the KDIGNIISDA/H-2D(b) complex induces autoimmune pathology in immunodeficient mice. We solved the X-ray crystal structure of the SALQNAASIA/H-2D(b) complex at 3.0 A resolution, and we modelled the KDIGNIISDA and SALQNAASI peptides in the H-2D(b) binding site. The structural analysis of the H-2D(b)-bound hsp60 epitopes offers insight into T-cell receptor cross-reactivity.
Structural analysis of mycobacterial and murine hsp60 epitopes in complex with the class I MHC molecule H-2Db.,Ciatto C, Capitani G, Tissot AC, Pecorari F, Pluckthun A, Grutter MG FEBS Lett. 2003 May 22;543(1-3):11-5. PMID:12753896[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ciatto C, Capitani G, Tissot AC, Pecorari F, Pluckthun A, Grutter MG. Structural analysis of mycobacterial and murine hsp60 epitopes in complex with the class I MHC molecule H-2Db. FEBS Lett. 2003 May 22;543(1-3):11-5. PMID:12753896
