Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations

Journal of Biological Chemistry

Volumn 279, Issue 6, 2004, Pages 4657-4662

  Suenaga, Atsushi ^a   Kiyatkin, Anatoly B ^b   Hatakeyama, Mariko ^a   Futatsugi, Noriyuki ^a   Okimoto, Noriaki ^c   Hirano, Yoshinori ^c   Narumi, Tetsu ^a   Kawai, Atsushi ^c   Susukita, Ryutaro ^c   Koishi, Takahiro ^c   Furusawa, Hideaki ^c   Yasuoka, Kenji ^d   Takada, Naoki ^a   Ohno, Yousuke ^a   Taiji, Makoto ^a   Ebisuzaki, Toshikazu ^c   Hoek, Jan B ^b   Konagaya, Akihiko ^a   Kholodenko, Boris N ^b  

^a RIKEN YOKOHAMA INSTITUTE   (Japan)

^b THOMAS JEFFERSON UNIVERSITY   (United States)

^c RIKEN   (Japan)

^d KEIO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; COMPUTER SIMULATION; MOLECULAR DYNAMICS; RIGIDITY;

PHOSPHORYLATION;

BIOCHEMISTRY;

ADAPTOR PROTEIN; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; TYROSINE;

ANIMAL CELL; ARTICLE; AUTOPHOSPHORYLATION; BINDING AFFINITY; CELL PROLIFERATION; CELL SURVIVAL; COUPLING FACTOR; DRUG RECEPTOR BINDING; MITOGENICITY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; SIMULATION; STRUCTURE ANALYSIS;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ADAPTOR PROTEINS, VESICULAR TRANSPORT; BINDING SITES; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN CONFORMATION; SRC HOMOLOGY DOMAINS; THERMODYNAMICS; TYROSINE;

ANIMALIA; VITIS SP.;

EID: 10744228882     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M310598200     Document Type: Article

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