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Search results 101 to 158 out of 158 for Msh3

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0.021s
Type Details Score
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Protein
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
UniProt Feature
Begin: 1
Description: DNA mismatch repair protein Msh3
Type: chain
End: 1091
Protein
Organism: Mus musculus/domesticus
Length: 129  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1091  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 101  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 56  
Fragment?: false
Publication
First Author: New L
Year: 1993
Journal: Mol Gen Genet
Title: The yeast gene MSH3 defines a new class of eukaryotic MutS homologues.
Volume: 239
Issue: 1-2
Pages: 97-108
DO Term
Publication
First Author: Geeta Vani R
Year: 1999
Journal: Genomics
Title: Cloning of rat MLH1 and expression analysis of MSH2, MSH3, MSH6, and MLH1 during spermatogenesis.
Volume: 62
Issue: 3
Pages: 460-7
Publication
First Author: Lipkin SM
Year: 2002
Journal: Nat Genet
Title: Meiotic arrest and aneuploidy in MLH3-deficient mice.
Volume: 31
Issue: 4
Pages: 385-90
Publication
First Author: Pinto RM
Year: 2013
Journal: PLoS Genet
Title: Mismatch repair genes Mlh1 and Mlh3 modify CAG instability in Huntington's disease mice: genome-wide and candidate approaches.
Volume: 9
Issue: 10
Pages: e1003930
Protein Domain
Type: Domain
Description: Mismatch repair contributes to the overall fidelity of DNA replication and is essential for combating the adverse effects of damage to the genome. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex. The post-replicative Mismatch Repair System (MMRS) of Escherichia coli involves MutS (Mutator S), MutL and MutH proteins, and acts to correct point mutations or small insertion/deletion loops produced during DNA replication []. MutS and MutL are involved in preventing recombination between partially homologous DNA sequences. The assembly of MMRS is initiated by MutS, which recognises and binds to mispaired nucleotides and allows further action of MutL and MutH to eliminate a portion of newly synthesized DNA strand containing the mispaired base []. MutS can also collaborate with methyltransferases in the repair of O(6)-methylguanine damage, which would otherwise pair with thymine during replication to create an O(6)mG:T mismatch []. MutS exists as a dimer, where the two monomers have different conformations and form a heterodimer at the structural level []. Only one monomer recognises the mismatch specifically and has ADP bound. Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure [], and is composed of:N-terminal mismatch-recognition domain, which is similar in structure to tRNA endonuclease.Connector domain, which is similar in structure to Holliday junction resolvase ruvC.Core domain, which is composed of two separate subdomains that join together to form a helical bundle; from within the core domain, two helices act as levers that extend towards (but do not touch) the DNA.Clamp domain, which is inserted between the two subdomains of the core domain at the top of the lever helices; the clamp domain has a β-sheet structure.ATPase domain (connected to the core domain), which has a classical Walker A motif.HTH (helix-turn-helix) domain, which is involved in dimer contacts.The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair. Homologues of MutS have been found in many species including eukaryotes (MSH 1, 2, 3, 4, 5, and 6 proteins), archaea and bacteria, and together these proteins have been grouped into the MutS family. Although many of these proteins have similar activities to the E. coli MutS, there is significant diversity of function among the MutS family members. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein [].This diversity is even seen within species, where many species encode multiple MutS homologues with distinct functions []. Inter-species homologues may have arisen through frequent ancient horizontal gene transfer of MutS (and MutL) from bacteria to archaea and eukaryotes via endosymbiotic ancestors of mitochondria and chloroplasts []. This entry represents the C-terminal domain found in proteins in the MutS family of DNA mismatch repair proteins. The C-terminal region of MutS is comprised of the ATPase domain and the HTH (helix-turn-helix)domain, the latter being involved in dimer contacts. Yeast MSH3 [], bacterial proteins involved in DNA mismatch repair, and the predicted protein product of the Rep-3 gene of mouse share extensive sequence similarity. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein.
Protein Domain
Type: Domain
Description: Mismatch repair contributes to the overall fidelity of DNA replication and is essential for combating the adverse effects of damage to the genome. It involves the correction of mismatched base pairs that have been missed by the proofreading element of the DNA polymerase complex. The post-replicative Mismatch Repair System (MMRS) of Escherichia coli involves MutS (Mutator S), MutL and MutH proteins, and acts to correct point mutations or small insertion/deletion loops produced during DNA replication []. MutS and MutL are involved in preventing recombination between partially homologous DNA sequences. The assembly of MMRS is initiated by MutS, which recognises and binds to mispaired nucleotides and allows further action of MutL and MutH to eliminate a portion of newly synthesized DNA strand containing the mispaired base []. MutS can also collaborate with methyltransferases in the repair of O(6)-methylguanine damage, which would otherwise pair with thymine during replication to create an O(6)mG:T mismatch []. MutS exists as a dimer, where the two monomers have different conformations and form a heterodimer at the structural level []. Only one monomer recognises the mismatch specifically and has ADP bound. Non-specific major groove DNA-binding domains from both monomers embrace the DNA in a clamp-like structure. Mismatch binding induces ATP uptake and a conformational change in the MutS protein, resulting in a clamp that translocates on DNA. MutS is a modular protein with a complex structure [], and is composed of:N-terminal mismatch-recognition domain, which is similar in structure to tRNA endonuclease.Connector domain, which is similar in structure to Holliday junction resolvase ruvC.Core domain, which is composed of two separate subdomains that join together to form a helical bundle; from within the core domain, two helices act as levers that extend towards (but do not touch) the DNA.Clamp domain, which is inserted between the two subdomains of the core domain at the top of the lever helices; the clamp domain has a β-sheet structure.ATPase domain (connected to the core domain), which has a classical Walker A motif.HTH (helix-turn-helix) domain, which is involved in dimer contacts.The MutS family of proteins is named after the Salmonella typhimurium MutS protein involved in mismatch repair. Homologues of MutS have been found in many species including eukaryotes (MSH 1, 2, 3, 4, 5, and 6 proteins), archaea and bacteria, and together these proteins have been grouped into the MutS family. Although many of these proteins have similar activities to the E. coli MutS, there is significant diversity of function among the MutS family members. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein [].This diversity is even seen within species, where many species encode multiple MutS homologues with distinct functions []. Inter-species homologues may have arisen through frequent ancient horizontal gene transfer of MutS (and MutL) from bacteria to archaea and eukaryotes via endosymbiotic ancestors of mitochondria and chloroplasts []. This entry represents the N-terminal domain of proteins in the MutS family of DNA mismatch repair proteins, as well as closely related proteins. The N-terminal domain of MutS is responsible for mismatch recognition and forms a 6-stranded mixed β-sheet surrounded by three α-helices, which is similar to the structure of tRNA endonuclease. Yeast MSH3 [], bacterial proteins involved in DNA mismatch repair, and the predicted protein product of the Rep-3 gene of mouse share extensive sequence similarity. Human MSH has been implicated in non-polyposis colorectal carcinoma (HNPCC) and is a mismatch binding protein.
Protein
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 258  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 190  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 422  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 394  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1094  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1095  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 935  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1095  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1358  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1358  
Fragment?: false
Publication
First Author: Eisen JA
Year: 1998
Journal: Nucleic Acids Res
Title: A phylogenomic study of the MutS family of proteins.
Volume: 26
Issue: 18
Pages: 4291-300
Publication
First Author: Jiricny J
Year: 1994
Journal: Trends Genet
Title: Colon cancer and DNA repair: have mismatches met their match?
Volume: 10
Issue: 5
Pages: 164-8
Publication
First Author: Lamers MH
Year: 2000
Journal: Nature
Title: The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch.
Volume: 407
Issue: 6805
Pages: 711-7
Publication
First Author: Mendillo ML
Year: 2007
Journal: J Biol Chem
Title: Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo.
Volume: 282
Issue: 22
Pages: 16345-54
Publication
First Author: Nag N
Year: 2007
Journal: J Mol Biol
Title: Altered dynamics of DNA bases adjacent to a mismatch: a cue for mismatch recognition by MutS.
Volume: 374
Issue: 1
Pages: 39-53
Publication
First Author: Miguel V
Year: 2007
Journal: Biochem Biophys Res Commun
Title: The C-terminal region of Escherichia coli MutS and protein oligomerization.
Volume: 360
Issue: 2
Pages: 412-7
Publication
First Author: Rye PT
Year: 2008
Journal: DNA Repair (Amst)
Title: Mismatch repair proteins collaborate with methyltransferases in the repair of O(6)-methylguanine.
Volume: 7
Issue: 2
Pages: 170-6
Publication
First Author: Lin Z
Year: 2007
Journal: Nucleic Acids Res
Title: The origins and early evolution of DNA mismatch repair genes--multiple horizontal gene transfers and co-evolution.
Volume: 35
Issue: 22
Pages: 7591-603
Protein
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 958  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 764  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 870  
Fragment?: false
Publication
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
Publication
First Author: Church DM
Year: 2009
Journal: PLoS Biol
Title: Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume: 7
Issue: 5
Pages: e1000112