1A1O

MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM

Summary for 1A1O

• Entry DOI: 10.2210/pdb1a1o/pdb
• Descriptor: HLA class I histocompatibility antigen, BW-53 B*5301 alpha chain, Beta-2-microglobulin, PEPTIDE LS6 (KPIVQYDNF), ... (4 entities in total)
• Functional Keywords: major histocompatibility antigen, mhc, hla, hla-b53, malaria, complex (antigen-peptide), complex (antigen-peptide) complex, complex (antigen/peptide)
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P30491; Secreted . Note=(Microbial infection) In the presence of M: P61769
• Total number of polymer chains: 3
• Total formula weight: 44878.82

Authors

Smith, K.J.,Reid, S.W.,Harlos, K.,Mcmichael, A.J.,Stuart, D.I.,Bell, J.I.,Jones, E.Y. (deposition date: 1997-12-11, release date: 1998-04-08, Last modification date: 2023-08-02)

Primary citation

Smith, K.J.,Reid, S.W.,Harlos, K.,McMichael, A.J.,Stuart, D.I.,Bell, J.I.,Jones, E.Y.
Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.
Immunity, 4:215-228, 1996

PubMed Abstract: The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.

PubMed: 8624812
DOI: 10.1016/S1074-7613(00)80430-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)