H
Huguette Pelletier
Researcher at University of California, San Diego
Publications - 9
Citations - 2981
Huguette Pelletier is an academic researcher from University of California, San Diego. The author has contributed to research in topics: DNA polymerase & DNA polymerase II. The author has an hindex of 9, co-authored 9 publications receiving 2916 citations. Previous affiliations of Huguette Pelletier include National Institutes of Health & University of Texas Medical Branch.
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Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP.
TL;DR: Two ternary complexes of rat DNA polymerase beta, a DNA template-primer, and dideoxycytidine triphosphate have been determined at 2.9 A and 3.6 A resolution, suggesting that the polymerase-DNA-ddCTP interactions are not affected by crystal packing forces.
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Crystal Structure of a Complex Between Electron Transfer Partners, Cytochrome c Peroxidase and Cytochrome c
Huguette Pelletier,Joseph Kraut +1 more
TL;DR: Although crystals of the two complexes grew under very different conditions and belong to different space groups, the two complex structures are closely similar, suggesting that cytochrome c interacts with its redox partners in a highly specific manner.
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Crystal structures of human DNA polymerase beta complexed with gapped and nicked DNA: evidence for an induced fit mechanism.
TL;DR: Crystal structures suggest that pol beta may enhance fidelity by an induced fit mechanism in which correct base pairing between template and incoming dNTP induces alignment of catalytic groups for catalysis (via thumb closure), but incorrect base pairing will not.
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Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism.
TL;DR: The two invariant aspartates found in all polymerase sequences and implicated in catalytic activity have the same geometric arrangement within structurally similar but topologically distinct palms, indicating that the polymerases have maintained, or possibly re-evolved, a common nucleotidyl transfer mechanism.
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Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity, and fidelity
TL;DR: Crystal structures of human pol beta complexed with blunt-ended segments of DNA show that, although the crystals belong to a different space group, the DNA is nevertheless bound in the pol beta binding channel in the same way as the DNA in previously reported structures of rat pol beta complexes with a template-primer and ddCTP.