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

Nat Struct Biol. 1997 Jul;4(7):527-31. doi: 10.1038/nsb0797-527.

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.

Publication types

  • Letter

MeSH terms

  • Abatacept
  • Amino Acid Sequence
  • Animals
  • Antigens, CD / metabolism*
  • Antigens, Differentiation / chemistry*
  • Antigens, Differentiation / genetics
  • Antigens, Differentiation / metabolism*
  • B7-1 Antigen / metabolism*
  • B7-2 Antigen
  • Binding Sites
  • CD28 Antigens / metabolism*
  • CTLA-4 Antigen
  • Conserved Sequence
  • Dimerization
  • Humans
  • Immunoconjugates*
  • Magnetic Resonance Spectroscopy / methods
  • Membrane Glycoproteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Solutions
  • Sulfides

Substances

  • Antigens, CD
  • Antigens, Differentiation
  • B7-1 Antigen
  • B7-2 Antigen
  • CD28 Antigens
  • CD86 protein, human
  • CTLA-4 Antigen
  • CTLA4 protein, human
  • Immunoconjugates
  • Membrane Glycoproteins
  • Solutions
  • Sulfides
  • Abatacept

Associated data

  • GENBANK/D49841
  • GENBANK/D49844
  • GENBANK/J02988
  • GENBANK/L15006
  • GENBANK/L22178
  • GENBANK/M34563
  • GENBANK/U37121
  • GENBANK/X05719
  • GENBANK/X55288
  • GENBANK/X67915
  • GENBANK/X93304
  • GENBANK/X93305