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• W2894850608 abstract "Infection by HIV-1 requires protein-protein interactions involving gp120, CD4 and CCR5. We have previously demonstrated that the transferred nuclear Overhauser effect (TRNOE), in combination with asymmetric deuteration of a protein and a peptide ligand can be used to detect intermolecular interactions in large protein complexes with molecular weights up to ~ 100 kDa. Here, using this approach, we reveal interactions between tyrosine residues of a 27-residue peptide corresponding to the N-terminal segment of the CCR5 chemokine receptor, and a dimeric extended core YU2 gp120 envelope protein of HIV-1 complexed with a CD4-mimic miniprotein. The TRNOE crosspeaks in the ternary complex were assigned to the specific Tyr protons in the CCR5 peptide and to methyl protons of isoleucine, leucine and/or valine residues of gp120. Site directed mutagenesis combined with selective deuteration and TRNOE resulted in the first discernment by a biophysical method of specific pairwise interactions between gp120 residues in the bridging sheet of gp120 and the N-terminus of CCR5." @default.
• W2894850608 created "2018-10-12" @default.
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• W2894850608 date "2018-10-20" @default.
• W2894850608 modified "2023-10-16" @default.
• W2894850608 title "Defining specific residue‐to‐residue interactions between the gp120 bridging sheet and the N‐terminal segment of<scp>CCR</scp>5: applications of transferred<scp>NOE NMR</scp>" @default.
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• W2894850608 doi "https://doi.org/10.1111/febs.14673" @default.
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• W2894850608 hasPublicationYear "2018" @default.
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