1RTH

HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES

Summary for 1RTH

• Entry DOI: 10.2210/pdb1rth/pdb
• Descriptor: HIV-1 REVERSE TRANSCRIPTASE, 6,11-DIHYDRO-11-ETHYL-6-METHYL-9-NITRO-5H-PYRIDO[2,3-B][1,5]BENZODIAZEPIN-5-ONE, ... (4 entities in total)
• Functional Keywords: hiv-1 reverse transcriptase, nucleotidyltransferase
• Biological source: Human immunodeficiency virus 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): P04585 P04585
• Total number of polymer chains: 2
• Total formula weight: 116292.29

Authors

Ren, J.,Esnouf, R.,Garman, E.,Somers, D.,Ross, C.,Kirby, I.,Keeling, J.,Darby, G.,Jones, Y.,Stuart, D.,Stammers, D. (deposition date: 1995-05-03, release date: 1996-04-03, Last modification date: 2024-10-09)

Primary citation

Ren, J.,Esnouf, R.,Garman, E.,Somers, D.,Ross, C.,Kirby, I.,Keeling, J.,Darby, G.,Jones, Y.,Stuart, D.
High resolution structures of HIV-1 RT from four RT-inhibitor complexes.
Nat.Struct.Biol., 2:293-302, 1995

PubMed Abstract: We have determined the structures of four complexes of HIV-1 reverse transcriptase with non-nucleoside inhibitors, three fully refined at high resolution. The highest resolution structure is of the RT-nevirapine complex which has an R-factor of 0.186 and a root-mean-square bond length deviation of 0.015 A for all data to 2.2 A. The structures reveal a common mode of binding for these chemically diverse compounds. The common features of binding are largely hydrophobic interactions and arise from induced shape complementarity achieved by conformational rearrangement of the enzyme and conformational/configurational rearrangement of the compounds.

PubMed: 7540934
DOI: 10.1038/nsb0495-293

Experimental method

X-RAY DIFFRACTION (2.2 Å)