1vru
From Proteopedia
(New page: 200px<br /> <applet load="1vru" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vru, resolution 2.4Å" /> '''HIGH RESOLUTION STRU...) |
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| - | [[Image:1vru.gif|left|200px]]<br /> | + | [[Image:1vru.gif|left|200px]]<br /><applet load="1vru" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1vru" size=" | + | |
caption="1vru, resolution 2.4Å" /> | caption="1vru, resolution 2.4Å" /> | ||
'''HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES'''<br /> | '''HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the structures of four complexes of HIV-1 reverse | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1VRU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with CYA and AAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http:// | + | 1VRU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=CYA:'>CYA</scene> and <scene name='pdbligand=AAP:'>AAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VRU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hiv-1 reverse transcriptase]] | [[Category: hiv-1 reverse transcriptase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:37:58 2008'' |
Revision as of 13:38, 21 February 2008
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HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES
Overview
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.
About this Structure
1VRU is a Protein complex structure of sequences from Human immunodeficiency virus 1 with and as ligands. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 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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