The Crystal Structure of a Pyrrolinone-Peptide Hybrid Ligand Bound to the Human Class II MHC Protein HLA-DR1

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• 作者：Kon Ho Lee ; Gary L. Olson ; David R. Bolin ; Andrew B. Benowitz ; Paul A. Sprengeler ; Amos B. Smith ; III ; Ralph F. Hirschmann ; and Don C. Wiley
• 刊名：Journal of the American Chemical Society
• 出版年：2000
• 出版时间：September 6, 2000
• 年：2000
• 卷：122
• 期：35
• 页码：8370 - 8375
• 全文大小：301K
• 年卷期：v.122,no.35(September 6, 2000)
• ISSN：1520-5126

文摘

The X-ray crystal structure of a complex between the human class II major histocompatibility complex(MHC) protein HLA-DR1 and a bispyrrolinone-peptide hybrid ligand has been determined to 2.7 Å resolution.The bispyrrolinone segment of the ligand closely mimics the polyproline type II conformation of peptideligands bound to class II MHC molecules, emphasizing the considerable versatility of this peptidomimeticscaffold. Most hydrogen bonds conserved in all peptide/class II complexes are formed, and the side chains ofthe bispyrrolinone segment project into the same spaces as those occupied by side chains of bound peptides.Molecular modeling used in the design of the hybrid ligand was remarkably accurate in predicting the observedmolecular interactions.