Abstract
The structure of an N-terminal fragment of CD4 has been determined to 2.4 A resolution. It has two tightly abutting domains connected by a continuous beta strand. Both have the immunoglobulin fold, but domain 2 has a truncated beta barrel and a non-standard disulphide bond. The binding sites for monoclonal antibodies, class II major histocompatibility complex molecules, and human immunodeficiency virus gp120 can be mapped on the molecular surface.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antibodies, Monoclonal / immunology
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Binding Sites
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CD4 Antigens / immunology
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CD4 Antigens / ultrastructure*
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Crystallography
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Epitopes
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HIV Envelope Protein gp120 / metabolism
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HLA-D Antigens / metabolism
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Humans
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Hydrogen Bonding
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments
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Protein Conformation
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Recombinant Proteins
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Structure-Activity Relationship
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X-Ray Diffraction
Substances
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Antibodies, Monoclonal
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CD4 Antigens
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Epitopes
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HIV Envelope Protein gp120
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HLA-D Antigens
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Peptide Fragments
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Recombinant Proteins