Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28

William J. Metzler, Jürgen Bajorath, William Fenderson, Shyh Yu Shaw, Keith L. Constantine, Joseph Naemura, Gina Leytze, Robert J. Peach, Thomas B. Lavoie, Luciano Mueller, Peter S. Linsley

研究成果: Article同行評審

104 引文 斯高帕斯(Scopus)

摘要

The structure of human CTLA-4 reveals that residues Met 99, Tyr 100 and Tyr 104 of the M99YPPPY104 motif are adjacent to a patch of charged surface residues on the A'GFCC face of the protein. Mutation of these residues, which are conserved in the CTLA-4/CD28 family, significantly reduces binding to CD80 and/or CD86, implicating this patch as a ligand binding site.

原文English
頁(從 - 到)527-531
頁數5
期刊Nature Structural Biology
4
發行號7
DOIs
出版狀態Published - 1997 一月 1

All Science Journal Classification (ASJC) codes

  • 結構生物學
  • 生物化學
  • 遺傳學

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