pubmed-article:12456667 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12456667 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:12456667 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:12456667 | lifeskim:mentions | umls-concept:C0121925 | lld:lifeskim |
pubmed-article:12456667 | pubmed:dateCreated | 2002-11-28 | lld:pubmed |
pubmed-article:12456667 | pubmed:abstractText | 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. | lld:pubmed |
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pubmed-article:12456667 | pubmed:language | eng | lld:pubmed |
pubmed-article:12456667 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:12456667 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:LeftonR SRS | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:JerinaDonald... | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:HughesStephen... | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:DasKalyanK | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:ArnoldEddyE | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:BoyerPaul LPL | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:SarafianosSte... | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:IlankumaranPa... | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:CorinEllenE | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:ClarkArthur... | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:TuskeSteveS | lld:pubmed |
pubmed-article:12456667 | pubmed:author | pubmed-author:BirktoftJens... | lld:pubmed |
pubmed-article:12456667 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12456667 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12456667 | pubmed:pagination | 6614-24 | lld:pubmed |
pubmed-article:12456667 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:12456667 | pubmed:articleTitle | Structures of HIV-1 reverse transcriptase with pre- and post-translocation AZTMP-terminated DNA. | lld:pubmed |
pubmed-article:12456667 | pubmed:affiliation | Center for Advanced Biotechnology and Medicine, 679 Hoes Lane, Piscataway, NJ 08854-5638, USA. | lld:pubmed |
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