Nature. 1991 Sep 26;353(6342):326-9.

Identification of self peptides bound to purified HLA-B27.

Jardetzky TS, Lane WS, Robinson RA, Madden DR, Wiley DC.

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Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.

Abstract

A pool of endogenous peptides bound to the human class I MHC molecule, HLA-B27, has been isolated. Microsequence analysis of the pool and of 11 HPLC-purified peptides provides information on the binding specificity of the HLA-B27 molecule. The peptides all seem to be nonamers, seven of which match to protein sequences in a database search. These self peptides derive from abundant cytosolic or nuclear proteins, such as histone, ribosomal proteins, and members of the 90K heat-shock protein family.

PMID:: 1922338; [PubMed - indexed for MEDLINE]

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Structures reported by this article

The Three-Dimensional Structure Of Hla-B27 At 2.1 Angstroms Resolution Suggests A General Mechanism For Tight Peptide Binding To Mhc

PDB: 1HSA

Source: Homo sapiens, synthetic construct

Method: X-Ray Diffraction

Resolution: 2.1 Å

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Identification of self peptides bound to purified HLA-B27.

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