Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release

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

Volumn 113, Issue 12, 2016, Pages E1615-E1624

  Liang, Fu Cheng ^a   Kroon, Gerard ^b   McAvoy, Camille Z ^a   Chi, Chris ^a   Wright, Peter E ^b   Shan, Shu Ou ^a  

^a California Institute of Technology   (United States)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Membrane protein biogenesis; Molecular chaperone; NMR spectroscopy; Protein dynamics; Signal recognition particle

Indexed keywords

CHAPERONE; CPSRP43 PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; ALBINO 3 PROTEIN, ARABIDOPSIS; ARABIDOPSIS PROTEIN; CHLOROPLAST PROTEIN; CPSRP43 PROTEIN, ARABIDOPSIS; HYBRID PROTEIN; LIGHT HARVESTING SYSTEM; PROTEIN BINDING; SIGNAL RECOGNITION PARTICLE; THYLAKOID MEMBRANE PROTEIN;

ARTICLE; BIOCHEMICAL ANALYSIS; CONTROLLED STUDY; LIGHT HARVESTING SYSTEM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN SECRETION; RELEASE ASSAY; AMINO ACID SEQUENCE; ARABIDOPSIS; BINDING SITE; CHEMISTRY; COMPARATIVE STUDY; METABOLISM; MOLECULAR GENETICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PROTEIN ANALYSIS; PROTEIN TERTIARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SOLUBILITY; STRUCTURE ACTIVITY RELATION; THYLAKOID;

AMINO ACID SEQUENCE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; BINDING SITES; CHLOROPLAST PROTEINS; LIGHT-HARVESTING PROTEIN COMPLEXES; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION MAPPING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL RECOGNITION PARTICLE; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP; THYLAKOID MEMBRANE PROTEINS; THYLAKOIDS;

EID: 84962298294     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1524777113     Document Type: Article

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