The RCAN carboxyl end mediates calcineurin docking-dependent inhibition via a site that dictates binding to substrates and regulators

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 15, 2009, Pages 6117-6122

  Martínez Martínez, Sara ^a   Genescà, Lali ^b,e   Rodríguez, Antonio ^a,c   Raya, Alicia ^b   Salichs, Eulàlia ^b   Were, Felipe ^a   López Maderuelo, María Dolores ^a   Redondo, Juan Miguel ^a   De La Luna, Susana ^b,d,f  

^a CENTRO NACIONAL DE INVESTIGACIONES CARDIOVASCULARES CNIC   (Spain)

^b CENTRO DE INVESTIGACIÓN BIOMÉDICA EN RED DE ENFERMEDADES RARAS CIBERER   (Spain)

^c UNIVERSIDAD AUTÓNOMA DE MADRID   (Spain)

^d INSTITUCIÓ CATALANA DE RECERCA I ESTUDIS AVANÇATS ICREA   (Spain)

^e INSTITUT D'OPTIQUE GRADUATE SCHOOL   (France)

^f CENTRE FOR GENOMIC REGULATION CRG   (Spain)

Author keywords

Cabin1; Docking interaction; NFAT; Phosphatase; PxIxIT

Indexed keywords

CALCINEURIN; CALCIUM ION; PROTEIN; RCAN PROTEIN; TRANSCRIPTION FACTOR NFAT; UNCLASSIFIED DRUG; VALINE; CALCINEURIN PHOSPHATASE; MUSCLE PROTEIN; PHOSPHATASE;

ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; EMBRYO; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; HYDROPHOBICITY; INHIBITION KINETICS; MUTATION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; METABOLISM; MOLECULAR GENETICS; MOUSE; NUCLEOTIDE SEQUENCE; PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CALCINEURIN; CELL LINE; CONSERVED SEQUENCE; HUMANS; HYDROPHOBICITY; MICE; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; PHOSPHORIC MONOESTER HYDROLASES; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY;

EID: 65549150814     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0812544106     Document Type: Article

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