Electrostatic interactions of peptides flanking the tyrosine kinase domain in the epidermal growth factor receptor provides a model for intracellular dimerization and autophosphorylation

Proteins: Structure, Function and Genetics

Volumn 62, Issue 4, 2006, Pages 1036-1043

  Aifa, Sami ^a   Miled, Nabil ^b   Frikha, Fakher ^b   Aniba, Mohamed R ^a   Svensson, Samuel P S ^c   Rebai, Ahmed ^a  

^a CENTRE DE BIOTECHNOLOGIE DE SFAX   (Tunisia)

^b UNIVERSITY OF SFAX   (Tunisia)

^c LINKÖPING UNIVERSITY   (Sweden)

Author keywords

Charge cluster; Conserved peptides; Dimer; ErbB; Monomer

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TYROSINE KINASE;

AMINO ACID ANALYSIS; ARTICLE; AUTOPHOSPHORYLATION; DIMERIZATION; HUMAN; INTRACELLULAR TRANSPORT; MOLECULAR MECHANICS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN INTERACTION; REGULATORY MECHANISM; STRUCTURE ANALYSIS;

ANIMALS; DIMERIZATION; ELECTROSTATICS; MODELS, MOLECULAR; MUTAGENESIS; PEPTIDES; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN-TYROSINE KINASES; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECOMBINANT PROTEINS; VERTEBRATES;

VERTEBRATA;

EID: 33644841289     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.20780     Document Type: Article

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