Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. (Q38295596)

1 September 2017

title

Asymmetric recognition of DNA local distortion. Structure-based functional studies of eukaryotic Msh2-Msh6. (English)

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1 September 2017

Drotschmann K

1

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1 September 2017

Yang W

2

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1 September 2017

Brownewell FE

3

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1 September 2017

Kool ET

4

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Kunkel TA

5

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1 September 2017

language of work or name

English

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publication date

18 October 2001

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Journal of Biological Chemistry

1 September 2017

published in

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1 September 2017

volume

276

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1 September 2017

issue

49

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1 September 2017

page(s)

46225-46229

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Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA

1 September 2017

cites work

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Requirement for Phe36 for DNA binding and mismatch repair by Escherichia coli MutS protein

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A human 200-kDa protein binds selectively to DNA fragments containing G.T mismatches

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hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha

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A mutation in the MSH6 subunit of the Saccharomyces cerevisiae MSH2-MSH6 complex disrupts mismatch recognition

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Mismatch recognition and DNA-dependent stimulation of the ATPase activity of hMutSalpha is abolished by a single mutation in the hMSH6 subunit

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Isolation of an hMSH2-p160 Heterodimer That Restores DNA Mismatch Repair to Tumor Cells

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MSH6, a Saccharomyces cerevisiae protein that binds to mismatches as a heterodimer with MSH2.

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hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6

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Solution structure of a DNA duplex containing a replicable difluorotoluene-adenine pair

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Interaction of Escherichia coli MutS and MutL at a DNA mismatch

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21 January 2018

Identifiers

DOI

10.1074/JBC.C100450200

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1 September 2017

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