3AVA
Crystal structures of novel allosteric peptide inhibitors of HIV integrase in the LEDGF binding site
Summary for 3AVA
Entry DOI | 10.2210/pdb3ava/pdb |
Related | 3AV9 3AVB 3AVC 3AVF 3AVG 3AVH 3AVI 3AVJ 3AVK 3AVL 3AVM 3AVN |
Related PRD ID | PRD_000818 |
Descriptor | Integrase, LEDGF peptide, SULFATE ION, ... (6 entities in total) |
Functional Keywords | protein-protein interactions, hiv, recombination-inhibitor complex, recombination/inhibitor |
Biological source | Human immunodeficiency virus type 1 (HIV-1) More |
Cellular location | Matrix 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 chains | 4 |
Total formula weight | 42817.46 |
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 citation | Rhodes, 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: 21850718DOI: 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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