MSH3

rdf:langString MSH3

rdf:langString left

rdf:langString IDL recognition by MutSβ. A close-up comparison of MSH3—IDL interaction and Taq MutS with a single unpaired base . DNA-binding domains and DNA in Loop4. Domains I and IV of MSH2 are shown in green and yellow, and MBD and clamp domains of MSH3 in blue and orange. Diagram of the protein-DNA interactions using the same color scheme as in . Space-filling model of four IDLs and their interaction with domain I of MSH2 and MBD of MSH3 . The base pairs surrounding the IDL are shown in light and dark pink. For Loop2 and Loop4, a back view looking into the minor groove is also shown.

rdf:langString MutSβ Binding sites for MSH3 and MSH2 Model of the hMSH2 consensus interaction with hMSH3 or hMSH6. The interaction regions of hMSH2 with hMSH3 and of hMSH2 with hMSH6 are shown in gray and they are connected with lines that illustrate the specificity of each region to their pairing partner. The nucleotide binding regions are shown as black boxes. The location of the HNPCC mutations tested in these studies are illustrated as black diamonds. The N-terminal region of MSH3 contact the N-terminal region of MSH2 aa 378-625. The C-terminal regions connect at aa 1050-1128 of MSH3 and aa 875-934 of MSH2. The binding regions on MSH2 are identical when binding to either MSH3 or MSH6.

rdf:langString DNA mismatch repair protein, MutS Homolog 3 (MSH3) is a human homologue of the bacterial mismatch repair protein MutS that participates in the mismatch repair (MMR) system. MSH3 typically forms the heterodimer MutSβ with MSH2 in order to correct long insertion/deletion loops and base-base mispairs in microsatellites during DNA synthesis. Deficient capacity for MMR is found in approximately 15% of colorectal cancers, and somatic mutations in the MSH3 gene can be found in nearly 50% of MMR-deficient colorectal cancers.