Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms

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

Volumn 109, Issue 9, 2012, Pages 3305-3310

  Hanawa Suetsugu, Kyoko ^a   Kukimoto Niino, Mutsuko ^a,b   Mishima Tsumagari, Chiemi ^a   Akasaka, Ryogo ^a   Ohsawa, Noboru ^a   Sekine, Shun Ichi ^a,c   Ito, Takuhiro ^a,c   Tochio, Naoya ^a   Koshiba, Seizo ^a   Kigawa, Takanori ^a,d   Terada, Takaho ^a,b   Shirouzu, Mikako ^a   Nishikimi, Akihiko ^b,e   Uruno, Takehito ^e   Katakai, Tomoya ^f   Kinashi, Tatsuo ^f   Kohda, Daisuke ^e   Fukui, Yoshinori ^b,e   Yokoyama, Shigeyuki ^a,b,c  

^a RIKEN   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

^d TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^e KYUSHU UNIVERSITY   (Japan)

^f KANSAI MEDICAL UNIVERSITY   (Japan)

Author keywords

CDM proteins; Immunology; NMR; Protein complex; X ray crystallography

Indexed keywords

DOCK2 PROTEIN; ELMO1 PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PROTEIN SH3; RAS PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; AUTOINHIBITION; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; HUMAN; INHIBITION KINETICS; MEMBRANE BINDING; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; GUANINE NUCLEOTIDE EXCHANGE FACTORS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, SECONDARY; RAC1 GTP-BINDING PROTEIN; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SRC HOMOLOGY DOMAINS;

EID: 84857751765     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1113512109     Document Type: Article

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