2k1c

From Proteopedia

Revision as of 12:06, 25 June 2008

Template:STRUCTURE 2k1c

NMR Structure of the C-terminal domain of HIV-1 Capsid in complex with peptide Inhibitor

Overview

The HIV-1 capsid protein plays a critical role in virus core particle assembly and is an important target for novel therapeutic strategies. In a previous study we characterized the binding affinity of a hydrocarbon stapled helical peptide, NYAD-1 for the capsid protein (Kd ~ 1 muM) and demonstrated its ability to penetrate the cell membrane. In cell based assays, NYAD-1 colocalized with the Gag polyprotein at the plasma membrane and disrupted the formation of mature and immature virus particles in vitro systems. Here, we complement the cellular and biochemical data with structural characterization of the interactions between the capsid and a soluble peptide analogue, NYAD-13. Solution NMR methods were used to determine a high resolution structure of the complex between the inhibitor and a monomeric form of the C-terminal domain of the capsid protein (mCA-CTD). The intermolecular interactions are mediated by the packing of hydrophobic side-chains at the buried interface and unperturbed by the presence of the olefinic chain on the solvent exposed surface of the peptide.

About this Structure

2K1C is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid., Bhattacharya S, Zhang H, Debnath AK, Cowburn D, J Biol Chem. 2008 Apr 21;. PMID:18417468

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