{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Acharya S"],"funding":["NCI NIH HHS","NIGMS NIH HHS"],"pagination":["13629-34"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC19374"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["93(24)"],"pubmed_abstract":["The genetic and biochemical properties of three human MutS homologues, hMSH2, hMSH3, and hMSH6, have been examined. The full-length hMSH6 cDNA and genomic locus were isolated and characterized, and it was demonstrated that the hMSH6 gene consisted of 10 exons and mapped to chromosome 2p15-16. The hMSH3 cDNA was in some cases found to contain a 27-bp deletion resulting in a loss of nine amino acids, depending on the individual from which the cDNA was isolated. hMSH2, hMSH3, and hMSH6 all showed similar tissue-specific expression patterns. hMSH2 protein formed a complex with both hMSH3 and hMSH6 proteins, similar to protein complexes demonstrated by studies of the Saccharomyces cerevisiae MSH2, MSH3, and MSH6. hMSH2 was also found to form a homomultimer complex, but neither hMSH3 nor hMSH6 appear to interact with themselves or each other. Analysis of the mismatched nucleotide-binding specificity of the hMSH2-hMSH3 and hMSH2-hMSH6 protein complexes showed that they have overlapping but not identical binding specificity. These results help to explain the distribution of mutations in different mismatch-repair genes seen in hereditary nonpolyposis colon cancer."],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6."],"pmcid":["PMC19374"],"funding_grant_id":["GM50006","P30 CA006516","R01 CA067007","R01 CA056542","R01 GM050006","CA 44704","CA 06516"],"pubmed_authors":["Acharya S","Wilson T","Kolodner R","Guerrette S","Fishel R","Kane MF","Marsischky GT","Gradia S"],"additional_accession":[]},"is_claimable":false,"name":"hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6.","description":"The genetic and biochemical properties of three human MutS homologues, hMSH2, hMSH3, and hMSH6, have been examined. The full-length hMSH6 cDNA and genomic locus were isolated and characterized, and it was demonstrated that the hMSH6 gene consisted of 10 exons and mapped to chromosome 2p15-16. The hMSH3 cDNA was in some cases found to contain a 27-bp deletion resulting in a loss of nine amino acids, depending on the individual from which the cDNA was isolated. hMSH2, hMSH3, and hMSH6 all showed similar tissue-specific expression patterns. hMSH2 protein formed a complex with both hMSH3 and hMSH6 proteins, similar to protein complexes demonstrated by studies of the Saccharomyces cerevisiae MSH2, MSH3, and MSH6. hMSH2 was also found to form a homomultimer complex, but neither hMSH3 nor hMSH6 appear to interact with themselves or each other. Analysis of the mismatched nucleotide-binding specificity of the hMSH2-hMSH3 and hMSH2-hMSH6 protein complexes showed that they have overlapping but not identical binding specificity. These results help to explain the distribution of mutations in different mismatch-repair genes seen in hereditary nonpolyposis colon cancer.","dates":{"release":"1996-01-01T00:00:00Z","publication":"1996 Nov","modification":"2024-11-06T23:52:31.969Z","creation":"2019-03-27T00:17:46Z"},"accession":"S-EPMC19374","cross_references":{"pubmed":["8942985"],"doi":["10.1073/pnas.93.24.13629"]}}