1vrt

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{{STRUCTURE_1vrt| PDB=1vrt | SCENE= }}
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'''HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES'''
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===HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES===
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==Overview==
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We have determined the structures of four complexes of HIV-1 reverse transcriptase with non-nucleoside inhibitors, three fully refined at high resolution. The highest resolution structure is of the RT-nevirapine complex which has an R-factor of 0.186 and a root-mean-square bond length deviation of 0.015 A for all data to 2.2 A. The structures reveal a common mode of binding for these chemically diverse compounds. The common features of binding are largely hydrophobic interactions and arise from induced shape complementarity achieved by conformational rearrangement of the enzyme and conformational/configurational rearrangement of the compounds.
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(as it appears on PubMed at http://www.pubmed.gov), where 7540934 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7540934}}
==About this Structure==
==About this Structure==
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[[Category: Stuart, D.]]
[[Category: Stuart, D.]]
[[Category: Hiv-1 reverse transcriptase]]
[[Category: Hiv-1 reverse transcriptase]]
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Revision as of 07:03, 29 July 2008

Image:1vrt.png

Template:STRUCTURE 1vrt

HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES

Template:ABSTRACT PUBMED 7540934

About this Structure

1VRT is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

High resolution structures of HIV-1 RT from four RT-inhibitor complexes., Ren J, Esnouf R, Garman E, Somers D, Ross C, Kirby I, Keeling J, Darby G, Jones Y, Stuart D, et al., Nat Struct Biol. 1995 Apr;2(4):293-302. PMID:7540934

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