1WIP

STRUCTURE OF T-CELL SURFACE GLYCOPROTEIN CD4, MONOCLINIC CRYSTAL FORM

Summary for 1WIP

• Entry DOI: 10.2210/pdb1wip/pdb
• Descriptor: T-CELL SURFACE GLYCOPROTEIN CD4 (1 entity in total)
• Functional Keywords: immunoglobulin fold, transmembrane, glycoprotein, t-cell, mhc lipoprotein, polymorphism
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01730
• Total number of polymer chains: 2
• Total formula weight: 80910.95

Authors

Wu, H.,Kwong, P.D.,Hendrickson, W.A. (deposition date: 1996-12-18, release date: 1997-07-07, Last modification date: 2024-11-20)

Primary citation

Wu, H.,Kwong, P.D.,Hendrickson, W.A.
Dimeric association and segmental variability in the structure of human CD4.
Nature, 387:527-530, 1997

PubMed Abstract: CD4 is a co-receptor in the cellular immune response. It increases the avidity of association between a T cell and an antigen-presenting cell by interacting with non-polymorphic portions of the complex between class II major histocompatibility complex (MHC) and T-cell receptor (TCR) molecules, and it contributes directly to signal transduction through its cytoplasmic association with the lymphocyte kinase Lck. CD4 also serves as the high-affinity receptor for cellular attachment and entry of the human immunodeficiency virus (HIV). The extracellular portion of CD4 comprises four immunoglobulin-like domains (D1-D4). This part of human CD4 (residues 1-369) has been characterized as a recombinant soluble protein (sCD4), and crystal structures have been described for the human D1D2 fragment and for the rat D3D4 fragment. We have now determined the structures of intact sCD4 in three crystal lattices. These structures have a hinge-like variability at the D1D2 to D3D4 junction that might be important in immune recognition and HIV fusion, and a common dimeric association through D4 domains. Dynamic light scattering measurements and chemical crosslinking of sCD4 corroborate dimerization at high protein concentration. We suggest that such dimers mayhave relevance as mediators of signal transduction in T cells.

PubMed: 9168119
DOI: 10.1038/387527a0

Experimental method

X-RAY DIFFRACTION (4 Å)