2k1c
From Proteopedia
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'''NMR Structure of the C-terminal domain of HIV-1 Capsid in complex with peptide Inhibitor''' | '''NMR Structure of the C-terminal domain of HIV-1 Capsid in complex with peptide Inhibitor''' | ||
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| + | ==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== | ==About this Structure== | ||
2K1C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K1C OCA]. | 2K1C is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K1C OCA]. | ||
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| + | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/18417468 18417468] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
[[Category: Zinc-finger]] | [[Category: Zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 30 13:29:26 2008'' |
Revision as of 10:29, 30 April 2008
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 Page seeded by OCA on Wed Apr 30 13:29:26 2008
Categories: Human immunodeficiency virus 1 | Protein complex | Bhattacharya, S. | Cowburn, D. | Debnath, A K. | Zhang, H. | Aid | Alpha-helix | Aspartyl protease | Capsid maturation | Capsid protein | Cytoplasm | Dna integration | Dna recombination | Dna-directed dna polymerase | Endonuclease | Hydrocarbon stapling | Hydrolase | Lipoprotein | Magnesium | Membrane | Metal-binding | Multifunctional enzyme | Myristate | Nuclease | Nucleotidyltransferase | Nucleus | Phosphoprotein | Protease | Ribosomal frameshifting | Rna-binding | Rna-directed dna polymerase | Transferase | Viral nucleoprotein | Viral protein | Virion | Zinc | Zinc-finger
