2RLL

CCR5 Nt(7-15)

Summary for 2RLL

• Entry DOI: 10.2210/pdb2rll/pdb
• Descriptor: 9-mer from C-C chemokine receptor type 5 (1 entity in total)
• Functional Keywords: hiv-1 coreceptor ccr5 n-terminus bound to gp120:cd4, g-protein coupled receptor, glycoprotein, host-virus interaction, membrane, polymorphism, sulfation, transducer, transmembrane, membrane protein
• Cellular location: Cell membrane; Multi-pass membrane protein: P51681
• Total number of polymer chains: 1
• Total formula weight: 1307.36

Authors

Bewley, C.A.,Lam, S.N. (deposition date: 2007-07-21, release date: 2007-09-25, Last modification date: 2024-10-30)

Primary citation

Huang, C.-C.,Lam, S.N.,Acharya, P.,Tang, M.,Xiang, S.-H.,Hussan, S.S.,Stanfield, R.L.,Robinson, J.,Sodroski, J.,Wilson, I.A.,Wyatt, R.,Bewley, C.A.,Kwong, P.D.
Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4
Science, 317:1930-1934, 2007

PubMed Abstract: The CCR5 co-receptor binds to the HIV-1 gp120 envelope glycoprotein and facilitates HIV-1 entry into cells. Its N terminus is tyrosine-sulfated, as are many antibodies that react with the co-receptor binding site on gp120. We applied nuclear magnetic resonance and crystallographic techniques to analyze the structure of the CCR5 N terminus and that of the tyrosine-sulfated antibody 412d in complex with gp120 and CD4. The conformations of tyrosine-sulfated regions of CCR5 (alpha-helix) and 412d (extended loop) are surprisingly different. Nonetheless, a critical sulfotyrosine on CCR5 and on 412d induces similar structural rearrangements in gp120. These results now provide a framework for understanding HIV-1 interactions with the CCR5 N terminus during viral entry and define a conserved site on gp120, whose recognition of sulfotyrosine engenders posttranslational mimicry by the immune system.

PubMed: 17901336
DOI: 10.1126/science.1145373

Experimental method

SOLUTION NMR