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Matches in SemOpenAlex for { <https://semopenalex.org/work/W2010271504> ?p ?o ?g. }

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• W2010271504 startingPage "749" @default.
• W2010271504 abstract "Substrate-induced conformational change of the protein is the linchpin of enzymatic reactions. Replicative DNA polymerases, for example, convert from an open to a closed conformation in response to dNTP binding. Human DNA polymerase-iota (hPoliota), a member of the Y family of DNA polymerases, differs strikingly from other polymerases in its much higher proficiency and fidelity for nucleotide incorporation opposite template purines than opposite template pyrimidines. We present here a crystallographic analysis of hPoliota binary complexes, which together with the ternary complexes show that, contrary to replicative DNA polymerases, the DNA, and not the polymerase, undergoes the primary substrate-induced conformational change. The incoming dNTP pushes templates A and G from the anti to the syn conformation dictated by a rigid hPoliota active site. Together, the structures posit a mechanism for template selection wherein dNTP binding induces a conformational switch in template purines for productive Hoogsteen base pairing." @default.
• W2010271504 created "2016-06-24" @default.
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• W2010271504 date "2006-04-01" @default.
• W2010271504 modified "2023-10-12" @default.
• W2010271504 title "An Incoming Nucleotide Imposes an anti to syn Conformational Change on the Templating Purine in the Human DNA Polymerase-ι Active Site" @default.
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• W2010271504 doi "https://doi.org/10.1016/j.str.2006.01.010" @default.
• W2010271504 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16615915" @default.
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