Domain movement in gelsolin: A calcium-activated switch

Science

Volumn 286, Issue 5446, 1999, Pages 1939-1942

  Robinson, Robert C ^a   Mejillano, Marisan ^a   Le, Vincent P ^a   Burtnick, Leslie D ^a   Yin, Helen L ^a   Choe, Senyon ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM; GELSOLIN;

ACTIN FILAMENT; ARTICLE; BINDING SITE; CALCIUM BINDING; COMPLEX FORMATION; CYTOSKELETON; MODEL; PRIORITY JOURNAL; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

ACTINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GELSOLIN; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0033521081     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.286.5446.1939     Document Type: Article

References (20)

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18. 2, 0.5 mM dithiothreitol. Crystals were grown at 4°C from a protein sample (10 mg/ml) combined in a 1:1 ratio with a well solution consisting of 10% PEG 8000, 20% glycerol, and 100 mM Hepes (pH 7.5).
19. Atomic coordinates have been deposited in the Protein Data Bank (accession number 1DBO).
20. Supported by grants from the Heart and Stroke Foundation of British Columbia and Yukon (L.D.B.), National Institutes of Health (S.C., H.L.Y.), the American Heart Association (Texas) (H.L.Y.), and the Pioneer Fund and Hoffmann Foundation (R.C.R.). We thank W. Kwiatkowski for computing expertise and help with figure preparation, the ALS synchrotron source for help with data collection, S. Almo for supplying coordinates for yeast actin, and L. Blanchoin for gifts of actin.