Structural highlights
Function
[HA1L_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
MHC class I H-2Ld complexed with peptide QL9 (or p2Ca) is a high-affinity alloantigen for the 2C TCR. We used the crystal structure of H-2Ld with a mixture of bound peptides at 3.1 A to construct a model of the allogeneic 2C-Ld/QL9 complex for comparison with the syngeneic 2C-Kb/dEV8 structure. A prominent ridge on the floor of the Ld peptide-binding groove, not present in Kb, creates a C-terminal bulge in Ld peptides that greatly increases interactions with the 2C beta-chain. Furthermore, weak electrostatic complementarity between Asp77 on the alpha1 helix of Kb and 2C is enhanced in the allogeneic complex by closer proximity of QL9 peptide residue AspP8 to the 2C HV4 loop.
Structural basis of 2C TCR allorecognition of H-2Ld peptide complexes.,Speir JA, Garcia KC, Brunmark A, Degano M, Peterson PA, Teyton L, Wilson IA Immunity. 1998 May;8(5):553-62. PMID:9620676[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Speir JA, Garcia KC, Brunmark A, Degano M, Peterson PA, Teyton L, Wilson IA. Structural basis of 2C TCR allorecognition of H-2Ld peptide complexes. Immunity. 1998 May;8(5):553-62. PMID:9620676
