3CD4

REFINEMENT AND ANALYSIS OF THE FIRST TWO DOMAINS OF HUMAN CD4

Replaces:  2CD4

Summary for 3CD4

• Entry DOI: 10.2210/pdb3cd4/pdb
• Descriptor: T CELL SURFACE GLYCOPROTEIN CD4 (2 entities in total)
• Functional Keywords: t-cell surface glycoprotein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01730
• Total number of polymer chains: 1
• Total formula weight: 20200.97

Authors

Garrett, T.P.J.,Wang, J.,Yan, Y.,Harrison, S.C. (deposition date: 1992-07-30, release date: 1993-10-31, Last modification date: 2024-10-30)

Primary citation

Garrett, T.P.J.,Wang, J.,Yan, Y.,Liu, J.,Harrison, S.C.
Refinement and analysis of the structure of the first two domains of human CD4
J.Mol.Biol., 234:763-778, 1993

PubMed Abstract: The structure of a fragment of human CD4 containing two immunoglobulin (Ig)-like domains has been determined by X-ray crystallography and refined at 2.2 A resolution. The structure determination involved iterative building and simulated-annealing refinement, beginning with a partial model. Comparison of domain 1 with an Ig variable domain shows that CD4 has a long and prominent CDR2-like loop (the C"C" corner) and shortened CC' and FG loops (which mediate dimerization in IgV modules). Comparison of domain 2 with Ig modules and domain 1 shows that it can be described as a truncated Ig V domain, in which strands C" and D are deleted. The intersheet disulfide in domain 2 is absent, and there is an altered packing of the two beta-sheets together with a remodeling of the hydrophobic core. The interface between domains 1 and 2 is a lap joint with an extensive hydrophobic surface. The key features of domain 1 that contribute to the interface are found at corresponding positions in domain 2, leading us to propose that the contact between domains 2 and 3 will resemble the one between domains 1 and 2.

PubMed: 8254672
DOI: 10.1006/jmbi.1993.1625

Experimental method

X-RAY DIFFRACTION (2.2 Å)