1A1N

MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1

Summary for 1A1N

• Entry DOI: 10.2210/pdb1a1n/pdb
• Descriptor: HLA class I histocompatibility antigen, BW-53 B*5301 alpha chain, Beta-2-microglobulin, PEPTIDE VPLRPMTY, ... (4 entities in total)
• Functional Keywords: major histocompatibility antigen, mhc, hla, hla-b3501, hiv, nef, 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: P30685; Secreted . Note=(Microbial infection) In the presence of M: P61769
• Total number of polymer chains: 3
• Total formula weight: 44691.65

Authors

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

Primary citation

Smith, K.J.,Reid, S.W.,Stuart, D.I.,McMichael, A.J.,Jones, E.Y.,Bell, J.I.
An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501.
Immunity, 4:203-213, 1996

PubMed Abstract: The crystal structure of the human major histocompatibility complex class I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution. Comparison with the crystal structure of the closely related allele HLA B*5301 reveals the structural basis for the tyrosine specificity of the B*3501 F pocket. The structure also reveals a novel conformation of the 8-mer peptide within the binding groove. The positions of the peptide N and C termini are nonstandard, but the classic pattern of hydrogen bonding to nonpolymorphic MHC class I residues is maintained, at the N terminus by addition of a water molecule, and at the C terminus by a substantial shift in the alpha 2 helix.

PubMed: 8624811
DOI: 10.1016/S1074-7613(00)80429-X

Experimental method

X-RAY DIFFRACTION (2 Å)