1HSB

DIFFERENT LENGTH PEPTIDES BIND TO HLA-AW68 SIMILARLY AT THEIR ENDS BUT BULGE OUT IN THE MIDDLE

Summary for 1HSB

• Entry DOI: 10.2210/pdb1hsb/pdb
• Descriptor: MHC class I antigen, Beta-2-microglobulin, BOUND PEPTIDE FRAGMENT, ... (6 entities in total)
• Functional Keywords: histocompatibility antigen, immune system
• Cellular location: Membrane; Single-pass type I membrane protein: A6YT91; Secreted: P61769
• Total number of polymer chains: 3
• Total formula weight: 43423.10

Authors

Guo, H.-C.,Strominger, J.L.,Wiley, D.C. (deposition date: 1993-03-30, release date: 1993-10-31, Last modification date: 2024-10-30)

Primary citation

Guo, H.C.,Jardetzky, T.S.,Garrett, T.P.,Lane, W.S.,Strominger, J.L.,Wiley, D.C.
Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle.
Nature, 360:364-366, 1992

PubMed Abstract: We report here the determination and refinement to 1.9 A resolution by X-ray cryo-crystallography the structure of HLA-Aw68. The averaged image from the collection of bound, endogenous peptides clearly shows the atomic structure at the first three and last two amino acids in the peptides but no connected electron density in between. This suggests that bound peptides, held at both ends, take alternative pathways and could be of different lengths by bulging out in the middle. Peptides eluted from HLA-Aw68 include peptides of 9, 10 and 11 amino acids, a direct indication of the length heterogeneity of tightly bound peptides. Peptide sequencing shows relatively conserved 'anchor' residues at position 2 and the carboxy-terminal residue. Conserved binding sites for the peptide N and C termini at the ends of the class I major histocompatibility complex binding groove are apparently dominant in producing the long half-lives of peptide binding and the peptide-dependent stabilization of the class I molecule's structure.

PubMed: 1448153
DOI: 10.1038/360364a0

Experimental method

X-RAY DIFFRACTION (1.9 Å)