1mu2: Difference between revisions

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[[Image:1mu2.jpg|left|200px]]<br /><applet load="1mu2" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1mu2.jpg|left|200px]]
caption="1mu2, resolution 2.35&Aring;" />
 
'''CRYSTAL STRUCTURE OF HIV-2 REVERSE TRANSCRIPTASE'''<br />
{{Structure
|PDB= 1mu2 |SIZE=350|CAPTION= <scene name='initialview01'>1mu2</scene>, resolution 2.35&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [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]
|GENE= POL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])
}}
 
'''CRYSTAL STRUCTURE OF HIV-2 REVERSE TRANSCRIPTASE'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1MU2 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=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</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=1MU2 OCA].  
1MU2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU2 OCA].  


==Reference==
==Reference==
Structure of HIV-2 reverse transcriptase at 2.35-A resolution and the mechanism of resistance to non-nucleoside inhibitors., Ren J, Bird LE, Chamberlain PP, Stewart-Jones GB, Stuart DI, Stammers DK, Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14410-5. Epub 2002 Oct 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12386343 12386343]
Structure of HIV-2 reverse transcriptase at 2.35-A resolution and the mechanism of resistance to non-nucleoside inhibitors., Ren J, Bird LE, Chamberlain PP, Stewart-Jones GB, Stuart DI, Stammers DK, Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14410-5. Epub 2002 Oct 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12386343 12386343]
[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: GOL]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: aids]]
[[Category: aid]]
[[Category: drug design]]
[[Category: drug design]]
[[Category: hiv-2 reverse transcriptase]]
[[Category: hiv-2 reverse transcriptase]]
[[Category: polymerase]]
[[Category: polymerase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:00 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:48:11 2008''

Revision as of 10:48, 20 March 2008

File:1mu2.jpg


Drag the structure with the mouse to rotate
1mu2, resolution 2.35Å
Ligands: SO4 and GOL
Gene: POL (Human immunodeficiency virus 1)
Activity: RNA-directed DNA polymerase, with EC number 2.7.7.49
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF HIV-2 REVERSE TRANSCRIPTASE


Overview

The HIV-2 serotype of HIV is a cause of disease in parts of the West African population, and there is evidence for its spread to Europe and Asia. HIV-2 reverse transcriptase (RT) demonstrates an intrinsic resistance to non-nucleoside RT inhibitors (NNRTIs), one of two classes of anti-AIDS drugs that target the viral RT. We report the crystal structure of HIV-2 RT to 2.35 A resolution, which reveals molecular details of the resistance to NNRTIs. HIV-2 RT has a similar overall fold to HIV-1 RT but has structural differences within the "NNRTI pocket" at both conserved and nonconserved residues. The structure points to the role of sequence differences that can give rise to unfavorable inhibitor contacts or destabilization of part of the binding pocket at positions 101, 106, 138, 181, 188, and 190. We also present evidence that the conformation of Ile-181 compared with the HIV-1 Tyr-181 could be a significant contributory factor to this inherent drug resistance of HIV-2 to NNRTIs. The availability of a refined structure of HIV-2 RT will provide a stimulus for the structure-based design of novel non-nucleoside inhibitors that could be used against HIV-2 infection.

About this Structure

1MU2 is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Structure of HIV-2 reverse transcriptase at 2.35-A resolution and the mechanism of resistance to non-nucleoside inhibitors., Ren J, Bird LE, Chamberlain PP, Stewart-Jones GB, Stuart DI, Stammers DK, Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14410-5. Epub 2002 Oct 17. PMID:12386343

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