An open and closed case for all polymerases. NLM AIDSLINE Important note: Information in this article was accurate in 1999. The state of the art may have changed since the publication date.

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An open and closed case for all polymerases.

Structure. 1999 Feb 15;7(2):R31-5. Unique Identifier : AIDSLINE MED/99148132
Doublie S; Sawaya MR; Ellenberger T; Department of Microbiology and Molecular Genetics, The Markey; Center for Molecular Genetics, University of Vermont, Burlington,; VT 05405, USA.

Abstract: The recently determined structures of HIV-1 reverse transcriptase and Taq DNA polymerase in complex with DNA primer-template and an incoming nucleotide have shown that a large conformational change configures the polymerase active site for nucleotidyl transfer. The structure of reverse transcriptase in the catalytic complex will open the path to the rational design of novel nucleoside analog inhibitors of viral replication.
Keywords: JOURNAL ARTICLE REVIEW REVIEW, TUTORIAL Binding Sites DNA Primers/CHEMISTRY DNA-Directed DNA Polymerase/*CHEMISTRY HIV-1/*ENZYMOLOGY HIV-1 Reverse Transcriptase/CHEMISTRY Models, Molecular Protein Structure, Secondary Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Taq Polymerase/CHEMISTRYKWDjournalarticlereviewreview,tutorialbindingsitesdnaprimers/chemistrydna-directeddnapolymerase/KWDchemistryhiv-1/KWDenzymologyhiv-1reversetranscriptase/chemistrymodels,molecularproteinstructure,secondarysupport,non-uKWDsKWDgov'tsupport,uKWDsKWDgov't,pKWDhKWDsKWDtaqpolymerase/chemistry
990630
A9960986

Copyright © 1999 - National Library of Medicine. Reproduced under license with the National Library of Medicine, Bethesda, MD.

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