1CDI

STRUCTURES OF AN HIV AND MHC BINDING FRAGMENT FROM HUMAN CD4 AS REFINED IN TWO CRYSTAL LATTICES

Summary for 1CDI

• Entry DOI: 10.2210/pdb1cdi/pdb
• Descriptor: T CELL SURFACE GLYCOPROTEIN CD4 (1 entity in total)
• Functional Keywords: t-cell surface glycoprotein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 19826.52

Authors

Ryu, S.E.,Truneh, A.,Sweet, R.W.,Hendrickson, W.A. (deposition date: 1994-01-26, release date: 1994-04-30, Last modification date: 2024-10-30)

Primary citation

Ryu, S.E.,Truneh, A.,Sweet, R.W.,Hendrickson, W.A.
Structures of an HIV and MHC binding fragment from human CD4 as refined in two crystal lattices.
Structure, 2:59-74, 1994

PubMed Abstract: The T-cell surface glycoprotein CD4 interacts with class II molecules of the major histocompatibility complex (MHC) enhancing the signal for T-cell activation. Human CD4 also interacts, at high affinity, with the HIV envelope glycoprotein, gp120, to mediate T-cell infection by HIV. Crystal structures of amino-terminal two-domain (D1D2) fragments of human CD4, which contain the residues implicated in HIV and MHC interactions, have been reported earlier.

PubMed: 8075984
DOI: 10.1016/S0969-2126(00)00008-3

Experimental method

X-RAY DIFFRACTION (2.9 Å)