Crystal structure at 3.5 Å resolution of HIV-1 reverse transcriptase complexed with an inhibitor

A 3.5 angstrom resolution electron density map of the HIV-1 reverse transcriptase heterodimer complexed with nevirapine, a drug with potential for treatment of AIDS, reveals an asymmetric dimer. The polymerase (pol) domain of the 66-kilodalton subunit has a large cleft analogous to that of the Kleno...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1992-06, Vol.256 (5065), p.1783-1790
Hauptverfasser:	KOHLSTAEDT, L. A, WANG, J, FRIEDMAN, J. M, RICE, P. A, STEITZ, T. A
Format:	Artikel
Sprache:	eng
Schlagworte:	AIDS/HIV Azepines - pharmacology Binding Sites Biological and medical sciences Crystallography DNA Polymerase I - chemistry Escherichia coli - genetics Fundamental and applied biological sciences. Psychology HIV-1 - enzymology Microbiology Models, Molecular Molecular Structure Morphology, structure, chemical composition, physicochemical properties Nevirapine Protein Conformation Pyridines - pharmacology RNA-Directed DNA Polymerase - chemistry Virology
Online-Zugang:	Volltext
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