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The nucleotide binding properties of human MSH2/MSH3 are lesion-dependent and distinct from those of human MSH2/MSH6

Here, we report that MSH2/MSH3 maintains lesion specificity for small loops by a distinctly different mechanism than does MHSH2/MSH6 for single base mismatches. ADP and ATP have no preference for the subunits of hMSH2/MSH3. Upon lesion binding, however, hMSH2/MSH3 adopts a single “nucleotide signatu...

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Библиографические подробности
Главные авторы: Owen, Barbara A. L., Lang, Walter, McMurray, Cynthia T.
Формат: Artigo
Язык:Inglês
Опубликовано: 2009
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2982795/
https://ncbi.nlm.nih.gov/pubmed/19377479
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nsmb.1596
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