Mechanism for the selective interaction of C-terminal Eps15 Homology Domain Proteins With Specific Asn-Pro-Phe-containing partners

Journal of Biological Chemistry

Volumn 285, Issue 12, 2010, Pages 8687-8694

  Kieken, Fabien ^a   Sharma, Mahak ^a   Jović, Marko ^a   Giridharan, Sai Srinivas Panapakkam ^a   Naslavsky, Naava ^a   Caplan, Steve ^a   Sorgen, Paul L ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; BINDING AFFINITIES; ENDOCYTIC RECYCLING; EPIDERMAL GROWTH FACTOR RECEPTORS; GLUTATHIONE-S-TRANSFERASE; HOMOLOGY DOMAIN; MAMMALIAN CELLS; MOLECULAR MECHANISM; N-TERMINALS; PARALOGS; POSITIVELY CHARGED; SALT BRIDGES; SELECTIVE INTERACTION; SOLUTION STRUCTURES; TRIPEPTIDE; TWO-HYBRID ANALYSIS;

AMINO ACIDS; BINDING ENERGY; MAMMALS; NUCLEAR MAGNETIC RESONANCE; PEPTIDES; PHOSPHATASES;

COMPLEXATION;

ASPARAGINE; EPIDERMAL GROWTH FACTOR RECEPTOR PATHWAY SUBSTRATE 15; PHENYLALANINE; PROLINE; CALCIUM BINDING PROTEIN; EPS15 PROTEIN, HUMAN; GLUTATHIONE TRANSFERASE; LYSINE; PHOSPHOPROTEIN; SIGNAL PEPTIDE;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENDOSOME; HUMAN; HUMAN CELL; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; TWO HYBRID SYSTEM;

MAMMALIA;

AMINO ACID SEQUENCE; ASPARAGINE; CALCIUM-BINDING PROTEINS; GLUTATHIONE TRANSFERASE; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LYSINE; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHENYLALANINE; PHOSPHOPROTEINS; PROLINE; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; TWO-HYBRID SYSTEM TECHNIQUES;

EID: 77950551801     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.045666     Document Type: Article

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