Structure of the full-length TRPV2 channel by cryo-EM

Nature Communications

Volumn 7, Issue , 2016, Pages

  Huynh, Kevin W ^a   Cohen, Matthew R ^a   Jiang, Jiansen ^b   Samanta, Amrita ^a   Lodowski, David T ^a   Zhou, Z Hong ^b   Moiseenkova Bell, Vera Y ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

VANILLOID RECEPTOR 2; ION; LIPID; TRPV1 PROTEIN, RAT; TRPV2 PROTEIN, RAT; VANILLOID RECEPTOR;

ELECTRON MICROSCOPY; ENZYME ACTIVITY; PHYSICOCHEMICAL PROPERTY; PROTEIN; RESOLUTION;

ANIMAL CELL; ARTICLE; BINDING SITE; BIOTINYLATION; CELL SURFACE; CONFORMATION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; HEAT; IMMUNOCYTOCHEMISTRY; ION TRANSPORT; NONHUMAN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; RAT; SEQUENCE ALIGNMENT; ANIMAL; CHEMISTRY; PERMEABILITY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; ULTRASTRUCTURE;

ANIMALS; BINDING SITES; CRYOELECTRON MICROSCOPY; IONS; LIPIDS; PERMEABILITY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RATS; TRPV CATION CHANNELS;

EID: 84962635518     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms11130     Document Type: Article

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