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

EMBO Journal

Volumn 17, Issue 9, 1998, Pages 2677-2686

  Iaccarino, Ingram ^a   Marra, Giancarlo ^a   Palombo, Fabio ^b   Jiricny, Josef ^a  

^a UNIVERSITY HOSPITAL ZURICH   (Switzerland)

^b IRBM   (Italy)

Author keywords

ATPase activity; hMutS ; Mismatch repair; Mismatch binding proteins

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ARGININE; GUANINE NUCLEOTIDE BINDING PROTEIN; LYSINE; OLIGONUCLEOTIDE; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DISSOCIATION CONSTANT; DNA REPAIR; ENZYME ACTIVITY; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; CONSERVED SEQUENCE; DIMERIZATION; DNA REPAIR; DNA-BINDING PROTEINS; ESCHERICHIA COLI; HUMANS; KINETICS; MACROMOLECULAR SUBSTANCES; MOLECULAR SEQUENCE DATA; MULTIDRUG RESISTANCE-ASSOCIATED PROTEINS; MUTAGENESIS, SITE-DIRECTED; MUTS HOMOLOG 2 PROTEIN; OLIGODEOXYRIBONUCLEOTIDES; POINT MUTATION; PROTO-ONCOGENE PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; STREPTOCOCCUS PNEUMONIAE;

EID: 0032079736     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.9.2677     Document Type: Article

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