The RAS-Binding Domain of Human BRAF Protein Serine/Threonine Kinase Exhibits Allosteric Conformational Changes upon Binding HRAS

Structure

Volumn 23, Issue 8, 2015, Pages 1382-1393

  Aramini, James M ^a,b   Vorobiev, Sergey M ^c   Tuberty, Lynda M ^a   Janjua, Haleema ^a,b   Campbell, Elliot T ^a   Seetharaman, Jayaraman ^c   Su, Min ^c   Huang, Yuanpeng J ^a,b   Acton, Thomas B ^a,b   Xiao, Rong ^a,b   Tong, Liang ^c   Montelione, Gaetano T ^a,b,d  

^a RUTGERS UNIVERSITY   (United States)

^b RUTGERS UNIVERSITY   (United States)

^c NONE   (United States)

^d RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

B RAF KINASE; HRAS PROTEIN; PROTEIN SERINE THREONINE KINASE; RAS PROTEIN; UNCLASSIFIED DRUG; BRAF PROTEIN, HUMAN; HRAS PROTEIN, HUMAN; PROTEIN BINDING; PROTEIN P21; RECOMBINANT PROTEIN;

ALLOSTERISM; ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DEUTERIUM HYDROGEN EXCHANGE; ENZYME ACTIVATION; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HUMAN; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE; R FACTOR; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; CRYSTALLIZATION; ESCHERICHIA COLI; GENE EXPRESSION; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; MOLECULAR MODEL; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; BINDING SITES; CLONING, MOLECULAR; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; GENE EXPRESSION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS B-RAF; PROTO-ONCOGENE PROTEINS P21(RAS); RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SIGNAL TRANSDUCTION;

EID: 84938742098     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.06.003     Document Type: Article

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