Specificity pockets for the side chains of peptide antigens in HLA-Aw68 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-12

AUTHORS

T P Garrett, M A Saper, P J Bjorkman, J L Strominger, D C Wiley

ABSTRACT

We have determined the structure of a second human histocompatibility glycoprotein, HLA-Aw68, by X-ray crystallography and refined it to a resolution of 2.6 A. Overall, the structure is extremely similar to that of HLA-A2 (refs 1, 2; and M.A.S. et al., manuscript in preparation), although the 11 amino-acid substitutions at polymorphic residues in the antigen-binding cleft alter the detailed shape and electrostatic charge of that site. A prominent negatively charged pocket within the cleft extends underneath the alpha-helix of the alpha 1-domain, providing a potential subsite for recognizing a positively charged side chain or peptide N terminus. Uninterpreted electron density, presumably representing an unknown 'antigen(s)', which seems to be different from that seen in the HLA-A2 structure, occupies the cleft and extends into the negatively charged pocket in HLA-Aw68. The structures of HLA-Aw68 and HLA-A2 demonstrate how polymorphism creates and alters subsites (pockets) positioned to bind peptide side chains, thereby suggesting the structural basis for allelic specificity in foreign antigen binding. More... »

PAGES

692-696

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/342692a0

DOI

http://dx.doi.org/10.1038/342692a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1015395588

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2594067


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