1E28

Nonstandard peptide binding of HLA-B*5101 complexed with HIV immunodominant epitope KM2(TAFTIPSI)

Summary for 1E28

• Entry DOI: 10.2210/pdb1e28/pdb
• Related: 1A1M 1A1N 1A1O 1A6Z 1A9B 1A9E 1AGB 1AGC 1AGD 1AGE 1AGF 1E27 1HLA 1HSA 1MHE 1TMC 2HLA 3HLA
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN HEAVY CHAIN, BETA-2 MICROGLOBULIN LIGHT CHAIN, PEPTIDE (3 entities in total)
• Functional Keywords: hla b51, hiv, mhc class i, histocompatibility complex
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 3
• Total formula weight: 44674.48

Authors

Maenaka, K.,Maenaka, T.,Tomiyama, H.,Takiguchi, M.,Stuart, D.I.,Jones, E.Y. (deposition date: 2000-05-18, release date: 2000-09-12, Last modification date: 2024-10-16)

Primary citation

Maenaka, K.,Maenaka, T.,Tomiyama, H.,Takiguchi, M.,Stuart, D.I.,Jones, E.Y.
Nonstandard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes.
J Immunol., 165:3260-3267, 2000

PubMed Abstract: The crystal structures of the human MHC class I allele HLA-B*5101 in complex with 8-mer, TAFTIPSI, and 9-mer, LPPVVAKEI, immunodominant peptide epitopes from HIV-1 have been determined by x-ray crystallography. In both complexes, the hydrogen-bonding network in the N-terminal anchor (P1) pocket is rearranged as a result of the replacement of the standard tyrosine with histidine at position 171. This results in a nonstandard positioning of the peptide N terminus, which is recognized by B*5101-restricted T cell clones. Unexpectedly, the P5 peptide residues appear to act as anchors, drawing the peptides unusually deeply into the peptide-binding groove of B51. The unique characteristics of P1 and P5 are likely to be responsible for the zig-zag conformation of the 9-mer peptide and the slow assembly of B*5101. A comparison of the surface characteristics in the alpha1-helix C-terminal region for B51 and other MHC class I alleles highlights mainly electrostatic differences that may be important in determining the specificity of human killer cell Ig-like receptor binding.

PubMed: 10975842
DOI: 10.4049/jimmunol.165.6.3260

Experimental method

X-RAY DIFFRACTION (3 Å)