Human TRPML1 channel structures in open and closed conformations

Nature

Volumn 550, Issue 7676, 2017, Pages

  Schmiege, Philip ^a,b   Fine, Michael ^b   Blobel, Günter ^a   Li, Xiaochun ^a,b,c  

^a ROCKEFELLER UNIVERSITY   (United States)

^b UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUND; CALCIUM CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL MUCOLIPIN 1; UNCLASSIFIED DRUG; APOPROTEIN; LIGAND; MCOLN1 PROTEIN, HUMAN;

CATION; CELLS AND CELL COMPONENTS; CHEMICAL BINDING; CYTOGENETICS; HOMEOSTASIS; PROTEIN;

ARTICLE; BINDING SITE; CRYOELECTRON MICROSCOPY; HUMAN; HYDROPHOBICITY; MUCOLIPIDOSIS TYPE 4; PATHOGENESIS; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; REGULATORY MECHANISM; STRUCTURE ANALYSIS; AGONISTS; CHEMICAL PHENOMENA; CHEMISTRY; METABOLISM; MOLECULAR MODEL; MUCOLIPIDOSIS; ULTRASTRUCTURE;

APOPROTEINS; BINDING SITES; CRYOELECTRON MICROSCOPY; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LIGANDS; MODELS, MOLECULAR; MUCOLIPIDOSES; PROTEIN CONFORMATION; TRANSIENT RECEPTOR POTENTIAL CHANNELS;

EID: 85031919260     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature24036     Document Type: Article

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