Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.

Journal article

The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the bet...

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Authors: Brady, R; Dodson, E; Dodson, G; Lange, G; Davis, S

• Publication status: Published
• Journal: Science (New York, N.Y.)
• Volume: 260
• Issue: 5110
• Pages: 979-983
• Publication date: 1993-05-01
• DOI: 10.1126/science.8493535
• EISSN: 1095-9203
• ISSN: 0036-8075
• Language: English
• Keywords: Molecular Sequence Data; Models, Molecular; Animals; Sequence Alignment; Rats; Protein Conformation; Crystallization; Humans; Amino Acid Sequence; Protein Folding; Protein Structure, Secondary; X-Ray Diffraction; Antigens, CD4