4iho
Crystal structure of H-2Db Y159F in complex with chimeric gp100Crystal structure of H-2Db Y159F in complex with chimeric gp100
Structural highlights
FunctionHA11_MOUSE Involved in the presentation of foreign antigens to the immune system. Publication Abstract from PubMedThe immunogenicity of H-2Db (Db )-restricted epitopes can be significantly increased by substituting peptide position 3 to a proline (p3P). The p3P modification enhances MHC stability without altering the conformation of the modified epitope allowing for T-cell cross-reactivity with the native peptide. The present study reveals how specific interactions between p3P and the highly conserved MHC heavy chain residue Y159 increase the stability of Db in complex with an optimized version of the melanoma-associated epitope gp10025 -33 . Furthermore, the p3P modification directly increased the affinity of the Db /gp10025 -33 -specific T-cell receptor (TCR) pMel. Surprisingly, the enhanced TCR binding was independent from the observed increased stability of the optimized Db /gp10025 -33 complex and from the interactions formed between p3P and Y159, indicating a direct effect of the p3P modification on TCR recognition. This article is protected by copyright. All rights reserved. Proline substitution independently enhances H-2D complex stabilization and TCR recognition of melanoma-associated peptides.,Uchtenhagen H, Abualrous ET, Stahl E, Allerbring EB, Sluijter M, Zacharias M, Sandalova T, van Hall T, Springer S, Nygren PA, Achour A Eur J Immunol. 2013 Aug 13. doi: 10.1002/eji.201343456. PMID:23939911[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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