Structural basis of the alternating-access mechanism in a bile acid transporter

Nature

Volumn 505, Issue 7484, 2014, Pages 569-573

  Zhou, Xiaoming ^a,b   Levin, Elena J ^a   Pan, Yaping ^a   McCoy, Jason G ^a   Sharma, Ruchika ^b   Kloss, Brian ^c   Bruni, Renato ^c   Quick, Matthias ^b,d   Zhou, Ming ^a,b,e  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

^b Och Spine at New York Presbyterian Hospitals   (United States)

^c New York Consortium on Membrane Protein Structure   (United States)

^d NEW YORK STATE PSYCHIATRIC INSTITUTE   (United States)

^e KUNMING INSTITUTE OF ZOOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BILE ACID; BILE ACID TRANSPORTER; CARRIER PROTEINS AND BINDING PROTEINS; TAUROCHOLIC ACID; UNCLASSIFIED DRUG;

ABSORPTION; BACTERIUM; BIOCHEMISTRY; CATION; CYTOLOGY; DIGESTIVE SYSTEM; HOMINID; MEMBRANE; PHYSIOLOGY; PROTEIN; SECRETION; SODIUM; TRANSLOCATION;

ARTICLE; BILE ACID SYNTHESIS; BINDING SITE; CONFORMATIONAL TRANSITION; CROSSING OVER; CRYSTAL STRUCTURE; CYTOPLASM; ENTEROHEPATIC CIRCULATION; ESCHERICHIA COLI; EXTRACELLULAR SPACE; HUMAN; HYDROGEN BOND; NEISSERIA MENINGITIDIS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; BILE ACIDS AND SALTS; BIOLOGICAL TRANSPORT; CARRIER PROTEINS; CELL MEMBRANE; CRYSTALLOGRAPHY, X-RAY; MEMBRANE GLYCOPROTEINS; MODELS, MOLECULAR; PROTEIN CONFORMATION; REPRODUCIBILITY OF RESULTS; ROTATION; SODIUM; STRUCTURE-ACTIVITY RELATIONSHIP; YERSINIA;

NEISSERIA MENINGITIDIS; YERSINIA FREDERIKSENII;

EID: 84892783318     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12811     Document Type: Article

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