English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors

Rittinger, K., Divita, G., & Goody, R. S. (1995). Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors. Proceedings of the National Academy of Sciences of the United States of America, 92(17), 8046-8049. Retrieved from http://www.jstor.org/stable/2368186.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-4E9C-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-4E9D-5
Genre: Journal Article
Alternative Title : Human immunodeficiency virus reverse transcriptase substrate-induced conformational changes and the mechanism of inhibition by nonnucleoside inhibitors

Files

show Files
hide Files
:
PNAS_92_1995_8046.pdf (Any fulltext), 888KB
 
File Permalink:
-
Name:
PNAS_92_1995_8046.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, Heidelberg; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Rittinger, Katrin1, Author              
Divita, Gilles1, Author              
Goody, Roger S.1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: A combination of transient kinetic and equilibrium titration methods has been used to show that both primer/template and nucleotide binding to human immunodeficiency virus type 1 (HIV-1) reverse transcriptase are two-step processes. In both cases, after initial formation of relatively weakly bound states, isomerization reactions lead to tightly bound states. In the case of deoxynucleotide binding to the reverse transcriptase-primer/template complex, the second step in the interaction is rate-limiting in the overall reaction during processive polymerization. Discrimination against incorrect nucleotides occurs both in the initial weak binding and in the second step but is purely kinetic in the second step (as opposed to thermodynamic in the first step). Nonnucleoside inhibitors have a relatively small effect on nucleotide-binding steps (overall affinity is reduced by a factor of ca. 10), while the affinity of the primer/template duplex is increased by at least a factor of 10. The major effect of nonnucleoside inhibitors is on the chemical step (nucleotide transfer).

Details

show
hide
Language(s): eng - English
 Dates: 1995-02-0219951995-05-03
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 665410
URI: http://www.jstor.org/stable/2368186
Other: 6606
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proceedings of the National Academy of Sciences of the United States of America
  Abbreviation : PNAS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 92 (17) Sequence Number: - Start / End Page: 8046 - 8049 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230