1N3N

Crystal structure of a mycobacterial hsp60 epitope with the murine class I MHC molecule H-2Db

Summary for 1N3N

• Entry DOI: 10.2210/pdb1n3n/pdb
• Descriptor: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B ALPHA CHAIN, BETA-2-MICROGLOBULIN, mycobacterial hsp60 decameric epitope, ... (5 entities in total)
• Functional Keywords: immunoglobulin fold, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01899; Secreted: P01887
• Total number of polymer chains: 12
• Total formula weight: 180670.12

Authors

Ciatto, C.,Capitani, G.,Tissot, A.C.,Pecorari, F.,Pluckthun, A.,Grutter, M.G. (deposition date: 2002-10-29, release date: 2003-05-27, Last modification date: 2011-07-13)

Primary citation

Ciatto, C.,Capitani, G.,Tissot, A.C.,Pecorari, F.,Plueckthun, A.,Gruetter, M.G.
Structural analysis of mycobacterial and murine hsp60 epitopes in complex with the class I MHC molecule H-2D(b)
FEBS Lett., 543:11-15, 2003

PubMed Abstract: 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.

PubMed: 12753896
DOI: 10.1016/S0014-5793(03)00325-9

Experimental method

X-RAY DIFFRACTION (3 Å)