1CID

CRYSTAL STRUCTURE OF DOMAINS 3 & 4 OF RAT CD4 AND THEIR RELATIONSHIP TO THE NH2-TERMINAL DOMAINS

Summary for 1CID

• Entry DOI: 10.2210/pdb1cid/pdb
• Descriptor: T CELL SURFACE GLYCOPROTEIN CD4, SULFATE ION (3 entities in total)
• Functional Keywords: t-cell surface glycoprotein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Membrane; Single-pass type I membrane protein: P05540
• Total number of polymer chains: 1
• Total formula weight: 19802.44

Authors

Brady, R.L.,Dodson, E.J.,Lange, G. (deposition date: 1993-01-28, release date: 1993-07-15, Last modification date: 2024-11-20)

Primary citation

Brady, R.L.,Dodson, E.J.,Dodson, G.G.,Lange, G.,Davis, S.J.,Williams, A.F.,Barclay, A.N.
Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains.
Science, 260:979-983, 1993

PubMed Abstract: 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.

PubMed: 8493535

Experimental method

X-RAY DIFFRACTION (2.8 Å)