A conserved MutS homolog connector domain interface interacts with MutL homologs

Escherichia coli MutS forms a mispair-dependent ternary complex with MutL that is essential for initiating mismatch repair (MMR) but is structurally uncharacterized, in part owing to its dynamic nature. Here, we used hydrogen/deuterium exchange mass spectrometry and other methods to identify a regio...

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Bibliografiska uppgifter
Huvudupphovsmän: Mendillo, Marc L., Hargreaves, Victoria V., Jamison, Jonathan W., Mo, Ashley O., Li, Sheng, Putnam, Christopher D., Woods, Virgil L., Kolodner, Richard D.
Materialtyp: Artigo
Språk:Inglês
Publicerad: National Academy of Sciences 2009
Ämnen:
Biological Sciences
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC2796910/
https://ncbi.nlm.nih.gov/pubmed/20080788
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0912250106
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