Binding thermodynamics of the N-terminal peptide of the CCR5 coreceptor to HIV-1 envelope glycoprotein gp120.

ABSTRACT: The initial events of HIV-1 cell infection involve the sequential binding of the viral envelope glycoprotein gp120 to the cellular CD4 receptor and the coreceptor, usually CCR5 or CXCR4. Binding to the coreceptor triggers the chain of events that culminates with the entry of the virus into the cell. In this process, the interaction of gp120 with the tyrosine-sulfated N-terminus of CCR5 is critical; however, this interaction has never been characterized at a quantitative or thermodynamic level. Here, we present the first thermodynamic analysis of the interaction of gp120 with the N-terminal peptide of the CCR5 coreceptor. Microcalorimetric titrations demonstrate that measurable binding of S22 peptide, a 22-amino acid tyrosine-sulfated peptide corresponding to the CCR5 N-terminus, requires p

SUBMITTER: Brower ET 

PROVIDER: S-EPMC2700308 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature