1cid
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CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS
OverviewOverview
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 beta sheets;, this results in an expansion of the domain. There is a difference of 30, degrees in the orientation between domains 3 and 4 when compared with, domains 1 and 2. The two CD4 fragment structures provide a basis from, which models of the overall receptor can be proposed. These models suggest, an extended structure comprising two rigid portions joined by a short and, possibly flexible linker region.
About this StructureAbout this Structure
1CID is a Single protein structure of sequence from Rattus norvegicus with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains., Brady RL, Dodson EJ, Dodson GG, Lange G, Davis SJ, Williams AF, Barclay AN, Science. 1993 May 14;260(5110):979-83. PMID:8493535
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