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.
MeSH terms
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Abatacept
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Amino Acid Sequence
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Animals
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Antigens, CD / metabolism*
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Antigens, Differentiation / chemistry*
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Antigens, Differentiation / genetics
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Antigens, Differentiation / metabolism*
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B7-1 Antigen / metabolism*
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B7-2 Antigen
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Binding Sites
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CD28 Antigens / metabolism*
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CTLA-4 Antigen
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Conserved Sequence
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Dimerization
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Humans
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Immunoconjugates*
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Magnetic Resonance Spectroscopy / methods
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Membrane Glycoproteins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Sequence Homology, Amino Acid
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Solutions
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Sulfides
Substances
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Antigens, CD
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Antigens, Differentiation
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B7-1 Antigen
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B7-2 Antigen
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CD28 Antigens
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CD86 protein, human
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CTLA-4 Antigen
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CTLA4 protein, human
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Immunoconjugates
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Membrane Glycoproteins
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Solutions
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Sulfides
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Abatacept
Associated data
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GENBANK/D49841
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GENBANK/D49844
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GENBANK/J02988
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GENBANK/L15006
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GENBANK/L22178
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GENBANK/M34563
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GENBANK/U37121
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GENBANK/X05719
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GENBANK/X55288
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GENBANK/X67915
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GENBANK/X93304
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GENBANK/X93305