3BC4
I84V HIV-1 protease in complex with a pyrrolidine diester
Summary for 3BC4
| Entry DOI | 10.2210/pdb3bc4/pdb |
| Descriptor | protease, 2-aminoethyl naphthalen-1-ylacetate, DIMETHYL SULFOXIDE, ... (4 entities in total) |
| Functional Keywords | protein-ligand complex, aids, aspartyl protease, capsid maturation, core protein, cytoplasm, dna integration, dna recombination, dna-directed dna polymerase, endonuclease, hydrolase, lipoprotein, magnesium, membrane, metal-binding, multifunctional enzyme, myristate, nuclease, nucleotidyltransferase, nucleus, phosphoprotein, protease, rna-binding, rna-directed dna polymerase, transferase, viral nucleoprotein, virion, zinc, zinc-finger |
| Biological source | Human immunodeficiency virus type 1 (Viruses) |
| 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): P03367 |
| Total number of polymer chains | 1 |
| Total formula weight | 11326.41 |
| Authors | Boettcher, J.,Blum, A.,Heine, A.,Diederich, W.E.,Klebe, G. (deposition date: 2007-11-12, release date: 2008-09-02, Last modification date: 2023-11-01) |
| Primary citation | Blum, A.,Heine, A.,Diederich, W.E.,Klebe, G. Targeting the open-flap conformation of HIV-1 protease with pyrrolidine-based inhibitors Chemmedchem, 3:1337-1344, 2008 Cited by PubMed Abstract: HIV protease is a well-established drug target in antiviral chemotherapy. Immense research efforts have been made to discover effective inhibitors, thus making the enzyme one of the most studied and best characterized proteins. Although the protease exhibits high flexibility, all approved drugs target virtually the same protein conformation. The development of viral cross-resistance demands the generation of inhibitors with novel scaffolds and deviating modes of binding. Herein we report the design and the short, high-yielding stereoselective synthesis of a series of chiral, symmetric pyrrolidine-based inhibitors targeting the open-flap conformation of the protease. The obtained co-crystal structure with one derivative provides a valuable starting point for further inhibitor design. PubMed: 18720485DOI: 10.1002/cmdc.200800113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.82 Å) |
Structure validation
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