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

Research output: Contribution to journalArticle

98 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)527-531
Number of pages5
JournalNature Structural Biology
Volume4
Issue number7
DOIs
Publication statusPublished - 1997 Jan 1

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

Fingerprint Dive into the research topics of 'Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28'. Together they form a unique fingerprint.

  • Cite this

    Metzler, W. J., Bajorath, J., Fenderson, W., Shaw, S. Y., Constantine, K. L., Naemura, J., Leytze, G., Peach, R. J., Lavoie, T. B., Mueller, L., & Linsley, P. S. (1997). Solution structure of human CTLA-4 and delineation of a CD80/CD86 binding site conserved in CD28. Nature Structural Biology, 4(7), 527-531. https://doi.org/10.1038/nsb0797-527