@article {697,
	title = {Activation in isolation: exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin},
	journal = {Febs Letters},
	volume = {552},
	number = {2-3},
	year = {2003},
	note = {ISI Document Delivery No.: 726DKTimes Cited: 15Cited Reference Count: 23},
	month = {Sep},
	pages = {82-85},
	type = {Article},
	abstract = {Gelsolin requires activation to carry out its severing and capping activities on F-actin. Here, we present the structure of the isolated C-terminal half of gelsolin (G4-G6) at 2.0 resolution in the presence of Ca2+ ions. This structure completes a triptych of the states of activation of G4-G6 that illuminates its role in the function of gelsolin. Activated G4-G6 displays an open conformation, with the actin-binding site on G4 fully exposed and all three type-2 Ca2+ sites occupied. Neither actin nor the type-1 Ca2+, which normally is sandwiched between actin and G4, is required to achieve this conformation. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.},
	keywords = {actin, calcium-activation, COMPLEX, DOMAINS, F-ACTIN, gelsolin, PLASMA GELSOLIN, REGULATORY PROTEIN, TRANSFORMATION},
	isbn = {0014-5793},
	url = {<Go to ISI>://000185583000002},
	author = {Narayan, K. and Chumnarnsilpa, S. and Choe, H. and Irobi, E. and Urosev, D. and Lindberg, U. and Schutt, C. E. and Burtnick, L. D. and Robinson, R. C.}
}
