Novel conserved hydrolase domain in the CLCA family of alleged calcium-activated chloride channels

Proteins: Structure, Function and Genetics

Volumn 63, Issue 3, 2006, Pages 424-439

  Pawłowski, Krzysztof ^a   Lepistö, Matti ^a   Meinander, Nina ^a   Sivars, Ulf ^a   Varga, Mikael ^a   Wieslander, Elisabet ^a  

^a ASTRAZENECA R AND D   (Sweden)

Author keywords

Calcium activated chloride channels; CLCA; Novel hydrolase; Structure modeling; Structure prediction; Zn2+ dependent metallohydrolases

Indexed keywords

CALCIUM ACTIVATED CHLORIDE CHANNEL; CALCIUM ACTIVATED CHLORIDE CHANNEL 1 HYDROLASE; CHLORIDE CHANNEL; HYDROLASE; MATRIX METALLOPROTEINASE; METALLOPROTEINASE; PROTEIN; PROTEINASE; STROMELYSIN 3; UNCLASSIFIED DRUG; ZINCIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CHLORIDE CONDUCTANCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE; GENETIC CONSERVATION; MAMMAL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CHLORIDE CHANNELS; CONSERVED SEQUENCE; HUMANS; HYDROLASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

CRUSTACEA; ECHINODERMATA; ESCHERICHIA COLI; HEXAPODA; MAMMALIA; METAZOA; PLATYHELMINTHES; UROCHORDATA; VERTEBRATA;

EID: 33646042261     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20887     Document Type: Article

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