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3AVA

Crystal structures of novel allosteric peptide inhibitors of HIV integrase in the LEDGF binding site

Summary for 3AVA
Entry DOI10.2210/pdb3ava/pdb
Related3AV9 3AVB 3AVC 3AVF 3AVG 3AVH 3AVI 3AVJ 3AVK 3AVL 3AVM 3AVN
Related PRD IDPRD_000818
DescriptorIntegrase, LEDGF peptide, SULFATE ION, ... (6 entities in total)
Functional Keywordsprotein-protein interactions, hiv, recombination-inhibitor complex, recombination/inhibitor
Biological sourceHuman immunodeficiency virus type 1 (HIV-1)
More
Cellular locationMatrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
Total number of polymer chains4
Total formula weight42817.46
Authors
Peat, T.S.,Deadman, J.J.,Newman, J.,Rhodes, D.I. (deposition date: 2011-03-02, release date: 2012-01-18, Last modification date: 2024-10-09)
Primary citationRhodes, D.I.,Peat, T.S.,Vandegraaff, N.,Jeevarajah, D.,Newman, J.,Martyn, J.,Coates, J.A.,Ede, N.J.,Rea, P.,Deadman, J.J.
Crystal structures of novel allosteric peptide inhibitors of HIV integrase identify new interactions at the LEDGF binding site.
Chembiochem, 12:2311-2315, 2011
Cited by
PubMed Abstract: An optimised method of solution cyclisation gave us access to a series of peptides including SLKIDNLD (2). We investigated the crystallographic complexes of the HIV integrase (HIV-IN) catalytic core domain with 13 of the peptides and identified multiple interactions at the binding site, including hydrogen bonds with residues Thr125 and Gln95, that have not previously been described as being accessible within the binding site. We show that the peptides inhibit the interaction of lens epithelium-derived growth factor (LEDGF) with HIV-IN in a proximity AlphaScreen assay and in an assay for the LEDGF enhancement of HIV-IN strand transfer. The interactions identified represent a potential framework for the development of new HIV-IN inhibitors.
PubMed: 21850718
DOI: 10.1002/cbic.201100350
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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