2000
DOI: 10.1006/jmbi.1999.3477
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Crystal structures of an N-terminal fragment from moloney murine leukemia virus reverse transcriptase complexed with nucleic acid: functional implications for template-primer binding to the fingers domain 1 1Edited by D. C. Rees

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Cited by 48 publications
(65 citation statements)
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“…As previously reported, K103A and R110A enzymes retain less than 10% of wild-type activity (2,3), while the remaining enzymes retain 40 to 70% of wild-type activity in the polyriboadenylate-oligodeoxyribosylthymine assay. However, despite their relatively high levels of activity on homopolymeric templates, all of the enzymes with substitutions for D114, R116, or N119 synthesized significantly less full-length product than the wild-type enzyme when assayed on an mRNA template, suggesting that they have processivity defects (25). In light of these findings regarding defects detectable in reconstituted reactions, it is not surprising that replication of viruses harboring these alterations was impaired.…”
Section: Discussionmentioning
confidence: 99%
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“…As previously reported, K103A and R110A enzymes retain less than 10% of wild-type activity (2,3), while the remaining enzymes retain 40 to 70% of wild-type activity in the polyriboadenylate-oligodeoxyribosylthymine assay. However, despite their relatively high levels of activity on homopolymeric templates, all of the enzymes with substitutions for D114, R116, or N119 synthesized significantly less full-length product than the wild-type enzyme when assayed on an mRNA template, suggesting that they have processivity defects (25). In light of these findings regarding defects detectable in reconstituted reactions, it is not surprising that replication of viruses harboring these alterations was impaired.…”
Section: Discussionmentioning
confidence: 99%
“…K103, R110, D114, R116, and N119 are highly conserved. Predictions suggest that K103 and R110 form hydrogen bonds with the incoming nucleotide (2,3,18,25). D114, R116, and N119 are involved in critical interactions of the primer-template with the fingers domain in crystal structures of the N-terminal fragment of MLV RT complexed with DNA.…”
Section: Discussionmentioning
confidence: 99%
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