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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bsg OCA], [http://pdbe.org/6bsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bsg RCSB], [http://www.ebi.ac.uk/pdbsum/6bsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bsg ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bsg OCA], [http://pdbe.org/6bsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bsg RCSB], [http://www.ebi.ac.uk/pdbsum/6bsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bsg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
HIV-1 reverse transcriptase (RT) contains both DNA polymerase and RNase H activities to convert the viral genomic RNA to dsDNA in infected host cells. Here we report the 2.65-A resolution structure of HIV-1 RT engaging in cleaving RNA in an RNA/DNA hybrid. A preferred substrate sequence is absolutely required to enable the RNA/DNA hybrid to adopt the distorted conformation needed to interact properly with the RNase H active site in RT. Substituting two nucleotides 4 bp upstream from the cleavage site results in scissile-phosphate displacement by 4 A. We also have determined the structure of HIV-1 RT complexed with an RNase H-resistant polypurine tract sequence, which adopts a rigid structure and is accommodated outside of the nuclease active site. Based on this newly gained structural information and a virtual drug screen, we have identified an inhibitor specific for the viral RNase H but not for its cellular homologs. | |||
Structure of HIV-1 reverse transcriptase cleaving RNA in an RNA/DNA hybrid.,Tian L, Kim MS, Li H, Wang J, Yang W Proc Natl Acad Sci U S A. 2018 Jan 16;115(3):507-512. doi:, 10.1073/pnas.1719746115. Epub 2018 Jan 2. PMID:29295939<ref>PMID:29295939</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 6bsg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:01, 25 April 2018
Structure of HIV-1 RT complexed with RNA/DNA hybrid in an RNA hydrolysis-off modeStructure of HIV-1 RT complexed with RNA/DNA hybrid in an RNA hydrolysis-off mode
Structural highlights
Publication Abstract from PubMedHIV-1 reverse transcriptase (RT) contains both DNA polymerase and RNase H activities to convert the viral genomic RNA to dsDNA in infected host cells. Here we report the 2.65-A resolution structure of HIV-1 RT engaging in cleaving RNA in an RNA/DNA hybrid. A preferred substrate sequence is absolutely required to enable the RNA/DNA hybrid to adopt the distorted conformation needed to interact properly with the RNase H active site in RT. Substituting two nucleotides 4 bp upstream from the cleavage site results in scissile-phosphate displacement by 4 A. We also have determined the structure of HIV-1 RT complexed with an RNase H-resistant polypurine tract sequence, which adopts a rigid structure and is accommodated outside of the nuclease active site. Based on this newly gained structural information and a virtual drug screen, we have identified an inhibitor specific for the viral RNase H but not for its cellular homologs. Structure of HIV-1 reverse transcriptase cleaving RNA in an RNA/DNA hybrid.,Tian L, Kim MS, Li H, Wang J, Yang W Proc Natl Acad Sci U S A. 2018 Jan 16;115(3):507-512. doi:, 10.1073/pnas.1719746115. Epub 2018 Jan 2. PMID:29295939[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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