AZT-resistant HIV-1 reverse transcriptase: Difference between revisions

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The exclusion mechanism also results from a set of mutations.  All amino acids involved in this mechanism exist in the finger or palm of [[reverse transcriptase]] in positions capable of affecting the binding of an incoming dNTP.  There is little known about this mechanism, however, evidence suggests that some mutations cause changes in the hydrogen bonding network between the deoxyribose of an incoming dNTP and the enzyme.  These changes increase the importance of the interactions of the enzyme with the 3'-OH and thus allow the mutant [[reverse transcriptase]] to better discriminate between normal dNTP which have 3'-OH and AZT which does not have a 3'-OH.
The exclusion mechanism also results from a set of mutations.  All amino acids involved in this mechanism exist in the finger or palm of [[reverse transcriptase]] in positions capable of affecting the binding of an incoming dNTP.  There is little known about this mechanism, however, evidence suggests that some mutations cause changes in the hydrogen bonding network between the deoxyribose of an incoming dNTP and the enzyme.  These changes increase the importance of the interactions of the enzyme with the 3'-OH and thus allow the mutant [[reverse transcriptase]] to better discriminate between normal dNTP which have 3'-OH and AZT which does not have a 3'-OH.
==3D structures of AZT-resistant HIV-1 reverse transcriptase==
[[3kli]] - P66/P51 (mutant)<br />
[[3kle]], [[3klg]], [[3klh]] – P66/P51 (mutant) + DNA


==References==
==References==

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexandra Clement, Michal Harel, Alexander Berchansky, David Canner