The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes

Journal of Molecular Biology

Volumn 426, Issue 1, 2014, Pages 150-168

  Skjevik, Åge Aleksander ^a,c   Mileni, Mauro ^b   Baumann, Anne ^a   Halskau, Øyvind ^a   Teigen, Knut ^a   Stevens, Raymond C ^b   Martinez, Aurora ^a  

^a UNIVERSITY OF BERGEN   (Norway)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

free energy of binding; molecular dynamics simulations; phospholipid bilayers; phosphorylation; X ray crystallography

Indexed keywords

PHOSPHATIDYLSERINE; PROTEIN 14 3 3; TYROSINE 3 MONOOXYGENASE; LIPOSOME; SERINE; SERINE 19; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DECOMPOSITION; ENZYME CONFORMATION; ENZYME PHOSPHORYLATION; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HYDROGEN BOND; MEMBRANE BINDING; MOLECULAR DYNAMICS; PHOSPHOLIPID BILAYER; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN PROCESSING; PROTEIN SECONDARY STRUCTURE; STRUCTURAL BIOINFORMATICS; X RAY CRYSTALLOGRAPHY; LIPOSOME MEMBRANE; MEMBRANE; MEMBRANE STRUCTURE; PROTEIN CONFORMATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SURFACE PLASMON RESONANCE;

EID: 84890857436     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.09.012     Document Type: Article

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