1n5y: Difference between revisions

Revision as of 07:56, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n5y.png

Template:STRUCTURE 1n5y

HIV-1 Reverse Transcriptase Crosslinked to Post-Translocation AZTMP-Terminated DNA (Complex P)HIV-1 Reverse Transcriptase Crosslinked to Post-Translocation AZTMP-Terminated DNA (Complex P)

Template:ABSTRACT PUBMED 12456667

About this StructureAbout this Structure

1N5Y is a Protein complex structure of sequences from Human immunodeficiency virus 1 and Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA., Sarafianos SG, Clark AD Jr, Das K, Tuske S, Birktoft JJ, Ilankumaran P, Ramesha AR, Sayer JM, Jerina DM, Boyer PL, Hughes SH, Arnold E, EMBO J. 2002 Dec 2;21(23):6614-24. PMID:12456667

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

OCA

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-'''HIV-1 Reverse Transcriptase Crosslinked to Post-Translocation AZTMP-Terminated DNA (Complex P)'''
+===HIV-1 Reverse Transcriptase Crosslinked to Post-Translocation AZTMP-Terminated DNA (Complex P)===
-==Overview==
+<!--
-AZT (3'-azido-3'-deoxythymidine) resistance involves the enhanced excision of AZTMP from the end of the primer strand by HIV-1 reverse transcriptase. This reaction can occur when an AZTMP-terminated primer is bound at the nucleotide-binding site (pre-translocation complex N) but not at the 'priming' site (post-translocation complex P). We determined the crystal structures of N and P complexes at 3.0 and 3.1 A resolution. These structures provide insight into the structural basis of AZTMP excision and the mechanism of translocation. Docking of a dNTP in the P complex structure suggests steric crowding in forming a stable ternary complex that should increase the relative amount of the N complex, which is the substrate for excision. Structural differences between complexes N and P suggest that the conserved YMDD loop is involved in translocation, acting as a springboard that helps to propel the primer terminus from the N to the P site after dNMP incorporation.
+The line below this paragraph, {{ABSTRACT_PUBMED_12456667}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12456667}}
 ==About this Structure==
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 [[Category: Nucleotide excision]]
 [[Category: Translocation]]
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