1LWF

CRYSTAL STRUCTURE OF A MUTANT HIV-1 REVERSE TRANSCRIPTASE (RTMQ+M184V: M41L/D67N/K70R/M184V/T215Y) IN COMPLEX WITH NEVIRAPINE

Summary for 1LWF

• Entry DOI: 10.2210/pdb1lwf/pdb
• Related: 1C0T 1C0U 1C1B 1C1C 1DTQ 1DTT 1EP4 1FK9 1FKO 1FKP 1JKH 1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LW0 1LW2 1LWC 1LWE 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7 1RTH 1RTI 1RTJ 1VRT 1VRU
• Descriptor: HIV-1 REVERSE TRANSCRIPTASE, 11-CYCLOPROPYL-5,11-DIHYDRO-4-METHYL-6H-DIPYRIDO[3,2-B:2',3'-E][1,4]DIAZEPIN-6-ONE, ... (4 entities in total)
• Functional Keywords: hiv-1 reverse transcriptase, aids, azt, 3tc, nrti, nevirapine, drug resistance mutations, transferase
• 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: 116338.29

Authors

Ren, J.,Chamberlain, P.P.,Nichols, C.E.,Douglas, L.,Stuart, D.I.,Stammers, D.K. (deposition date: 2002-05-31, release date: 2002-10-30, Last modification date: 2021-11-10)

Primary citation

Chamberlain, P.P.,Ren, J.,Nichols, C.E.,Douglas, L.,Lennerstrand, J.,Larder, B.A.,Stuart, D.I.,Stammers, D.K.
Crystal structures of Zidovudine- or Lamivudine-resistant human immunodeficiency virus type 1 reverse transcriptases containing mutations at codons 41, 184, and 215.
J.Virol., 76:10015-10019, 2002

PubMed Abstract: Six structures of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) containing combinations of resistance mutations for zidovudine (AZT) (M41L and T215Y) or lamivudine (M184V) have been determined as inhibitor complexes. Minimal conformational changes in the polymerase or nonnucleoside RT inhibitor sites compared to the mutant RTMC (D67N, K70R, T215F, and K219N) are observed, indicating that such changes may occur only with certain combinations of mutations. Model building M41L and T215Y into HIV-1 RT-DNA and docking in ATP that is utilized in the pyrophosphorolysis reaction for AZT resistance indicates that some conformational rearrangement appears necessary in RT for ATP to interact simultaneously with the M41L and T215Y mutations.

PubMed: 12208978
DOI: 10.1128/JVI.76.19.10015-10019.2002

Experimental method

X-RAY DIFFRACTION (2.8 Å)