Cryo-EM Structure of a KCNQ1/CaM Complex Reveals Insights into Congenital Long QT Syndrome

Cell

Volumn 169, Issue 6, 2017, Pages 1042-1050.e9

  Sun, Ji ^a   MacKinnon, Roderick ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

CaM; cryo EM; ion channel structure; KCNQ1; long QT syndrome; PIP2

Indexed keywords

CALMODULIN; POTASSIUM CHANNEL KCNQ1;

ARTICLE; CHEMICAL STRUCTURE; CONGENITAL LONG QT SYNDROME; CRYOELECTRON MICROSCOPY; GENE MUTATION; HUMAN; LONG QT SYNDROME; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; SEQUENCE ALIGNMENT; STEREOCHEMISTRY; XENOPUS LAEVIS; AMINO ACID SEQUENCE; ANIMAL; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR MODEL; MUTATION;

AMINO ACID SEQUENCE; ANIMALS; CALMODULIN; CRYOELECTRON MICROSCOPY; HUMANS; KCNQ1 POTASSIUM CHANNEL; LONG QT SYNDROME; MODELS, MOLECULAR; MUTATION; SEQUENCE ALIGNMENT; XENOPUS LAEVIS;

EID: 85020001894     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2017.05.019     Document Type: Article

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