@article {3920,
	title = {The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation},
	journal = {Cell},
	volume = {90},
	number = {4},
	year = {1997},
	note = {ISI Document Delivery No.: XT066Times Cited: 164Cited Reference Count: 50},
	month = {Aug},
	pages = {661-670},
	type = {Article},
	abstract = {The structure of gelsolin has been determined by crystallography and comprises six structurally related domains that, in a Ca2+-free environment, pack together to form a compact globular structure in which the putative actin-binding sequences are not sufficiently exposed to enable binding to occur. We propose that binding Ca2+ can release the connections that join the N- and C-terminal halves of gelsolin, enabling each half to bind actin relatively independently. Domain shifts are proposed in response to Ca2+ as bases for models of how gelsolin acts to sever, cap, or nucleate F-actin filaments. The structure also invites discussion of polyphosphoinositide binding to segment 2 and suggests how mutation at Asp-187 could initiate a series of events that lead to deposition of amyloid plaques, as observed in victims of familial amyloidosis (Finnish type).},
	keywords = {AMYLOIDOSIS, BINDING DOMAIN, calcium, DEFINITION, F-ACTIN, FILAMENT, IDENTIFICATION, PROTEIN, SEQUENCE, VILLIN},
	isbn = {0092-8674},
	url = {<Go to ISI>://A1997XT06600010},
	author = {Burtnick, L. D. and Koepf, E. K. and Grimes, J. and Jones, E. Y. and Stuart, D. I. and McLaughlin, P. J. and Robinson, R. C.}
}
