Abstract
In order for human immunodeficiency virus type 1 (HIV-1) to enter host cells, its envelope glycoprotein gp120 must bind to the host-cell surface receptor CD4 and to a co-receptor. An unusual posttranslational modification, tyrosine sulfation, is important to the co-receptor interaction. Huang et al . have investigated HIV-1 gp120 interactions with a sulfated N-terminal peptide from the co-receptor CCR5 and determined the crystal structure of a tyrosine-sulfated antibody in complex with gp120 and CD4. A conserved site in gp120 recognizes sulfo-tyrosine and might be a target for design of therapeutics. C.-c. Huang, S. N. Lam, P. Acharya, M. Tang, S.-H. Xiang, S. Shahzad-ul Hussan, R. L. Stanfield, J. Robinson, J. Sodroski, I. A. Wilson, R. Wyatt, C. A. Bewley, P. D. Kwong, Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science 317 , 1930-1934 (2007). [Abstract] [Full Text]
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