The interactions between gp120 and peptides corresponding to the N-terminal segment of the HIV-1 coreceptor CCR5 are being studied at atomic resolution using transferred-NOE and asymmetric deuteration of the components the ternary complex formed by gp120, a CD4 mimic peptide and Nt-CCR5 peptides. The structural information gained from this study could be applicable in developing HIV-1 entry inhibitors targeting the CCR5 binding site on gp120.
Using transferred-NOE and isotope-edited/isotope-filtered experiments on complexes in which the chemokine is uniformly labeled with 13C and the CCR5 peptide is unlabeled, we are studying the interactions CCL5 with the N-terminal segment of CCR5 that contains two sulfated tyrosine residues.
The interaction of regulatory phosphatases with the p38-MAPK will be explored by a variety of NMR methods. We believe that NMR spectroscopy is highly suitable for studying protein-protein interactions for complexes with low affinity such as the p38 complexes with KIM-peptides and with its specific phosphatases. Understanding the interaction between p38 and the KIM motif of phosphatases will be beneficial to understand the regulatory mechanisms for p38 MAPKs at atomic level resolution.