The mechanism of binding of the second PDZ domain from the Protein Tyrosine Phosphatase-BL to the Adenomatous Polyposis Coli tumor suppressor

Protein Engineering, Design and Selection

Volumn 27, Issue 8, 2014, Pages 249-253

  Di Silvio, Eva ^a   Bonetti, Daniela ^a   Toto, Angelo ^a   Morrone, Angela ^a   Gianni, Stefano ^a,b  

^a SAPIENZA UNIVERSITY OF ROME   (Italy)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

protein protein interaction

Indexed keywords

AMINO ACIDS; CELL ADHESION; DISSOCIATION; PHOSPHATASES; RATE CONSTANTS; TUMORS;

ADENOMATOUS POLYPOSIS COLI; BIOLOGICAL PROCESS; C-TERMINAL SEQUENCES; CONFORMATIONAL CHANGE; DISSOCIATION RATE CONSTANT; EXPERIMENTAL CONDITIONS; PLAUSIBLE MECHANISMS; PROTEIN-PROTEIN INTERACTIONS;

PROTEINS;

APC PROTEIN; NON RECEPTOR PROTEIN TYROSINE PHOSPHATASE 13; PEPTIDE; PROTEIN BINDING;

ARTICLE; BINDING KINETICS; DISSOCIATION; ENZYME CONFORMATION; ENZYME SUBSTRATE COMPLEX; PDZ DOMAIN; PRIORITY JOURNAL; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; METABOLISM; MOUSE; PROTEIN PROTEIN INTERACTION;

ADENOMATOUS POLYPOSIS COLI PROTEIN; ANIMALS; BINDING SITES; KINETICS; MICE; MODELS, MOLECULAR; PDZ DOMAINS; PEPTIDES; PROTEIN BINDING; PROTEIN INTERACTION MAPS; PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 13;

EID: 84906230429     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzu022     Document Type: Article

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