pubmed-article:17531814 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17531814 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:17531814 | lifeskim:mentions | umls-concept:C0072108 | lld:lifeskim |
pubmed-article:17531814 | lifeskim:mentions | umls-concept:C0879393 | lld:lifeskim |
pubmed-article:17531814 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:17531814 | pubmed:dateCreated | 2007-5-28 | lld:pubmed |
pubmed-article:17531814 | pubmed:abstractText | The eukaryotic MutS homolog complexes, Msh2-Msh6 and Msh2-Msh3, recognize mismatched bases in DNA during mismatch repair (MMR). The eukaryote-specific N-terminal regions (NTRs) of Msh6 and Msh3 have not been characterized other than by demonstrating that they contain an N-terminal PCNA-interacting motif. Here we have demonstrated genetically that the NTR of Msh6 has an important role in MMR that is partially redundant with PCNA binding. Small-angle X-ray scattering (SAXS) was used to determine the solution structure of the complex of PCNA with Msh2-Msh6 and with the isolated Msh6 NTR, revealing that the Msh6 NTR is a natively disordered domain that forms an extended tether between Msh6 and PCNA. Moreover, computational analysis of PCNA-interacting motifs in the S. cerevisiae proteome indicated that flexible linkers are a common theme for PCNA-interacting proteins that may serve to localize these binding partners without tightly restraining them to the immediate vicinity of PCNA. | lld:pubmed |
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pubmed-article:17531814 | pubmed:language | eng | lld:pubmed |
pubmed-article:17531814 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17531814 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:17531814 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17531814 | pubmed:month | May | lld:pubmed |
pubmed-article:17531814 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:17531814 | pubmed:author | pubmed-author:PutnamChristo... | lld:pubmed |
pubmed-article:17531814 | pubmed:author | pubmed-author:KolodnerRicha... | lld:pubmed |
pubmed-article:17531814 | pubmed:author | pubmed-author:ShellScarlet... | lld:pubmed |
pubmed-article:17531814 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:17531814 | pubmed:day | 25 | lld:pubmed |
pubmed-article:17531814 | pubmed:volume | 26 | lld:pubmed |
pubmed-article:17531814 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17531814 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17531814 | pubmed:pagination | 565-78 | lld:pubmed |
pubmed-article:17531814 | pubmed:dateRevised | 2011-3-18 | lld:pubmed |
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