UNC-45/CRO1/She4p (UCS) protein forms elongated dimer and joins two myosin heads near their actin binding region

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

Volumn 107, Issue 50, 2010, Pages 21382-21387

  Shi, Hang ^a   Blobel, Günter ^a  

^a ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Chaperone; Myosin stability; Processivity

Indexed keywords

ACTIN; ADENOSINE TRIPHOSPHATE; CRO1 PROTEIN; EPITOPE; FUNGAL PROTEIN; MYOSIN; SHE4P PROTEIN; UNC 45 PROTEIN; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; HYDROLYSIS; NONHUMAN; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN STRUCTURE;

ACTINS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CYTOSKELETAL PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MYOSINS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 78650730499     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1013038107     Document Type: Article

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