1rvr | pdb_00001rvr

USING NEVIRAPINE ANALOGS AS STRUCTURAL PROBES TO MODEL THEIR BINDING SITE ON HIV-1 REVERSE TRANSCRIPTASE

spinqualitylabelsall models 1rvr Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed Several molecular modeling techniques were used to generate an all-atom molecular model of a receptor binding site starting only from Ca atom coordinates. The model consists of 48 noncontiguous residues of the non-nucleoside binding site of HIV-1 reverse transcriptase and was generated using a congeneric series of nevirapine analogs as structural probes. On the basis of the receptor-ligand atom contacts, the program HINT was used to develop a 3D quantitative structure activity relationship that predicted the rank order of binding affinities for the series of inhibitors. Electronic profiles of the ligands in their docked conformations were characterized using electrostatic potential maps and frontier orbital calculations. These results led to the development of a 3D stereoelectronic pharmacophore which was used to construct 3D queries for database searches. A search of the National Cancer Institute's open database identified a lead compound that exhibited moderate antiviral activity. All-atom models for the non-nucleoside binding site of HIV-1 reverse transcriptase complexed with inhibitors: a 3D QSAR approach.,Gussio R, Pattabiraman N, Zaharevitz DW, Kellogg GE, Topol IA, Rice WG, Schaeffer CA, Erickson JW, Burt SK J Med Chem. 1996 Apr 12;39(8):1645-50. PMID:8648604 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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