@article {643,
	title = {From the first to the second domain of gelsolin: a common path on the surface of actin?},
	journal = {Febs Letters},
	volume = {552},
	number = {2-3},
	year = {2003},
	note = {ISI Document Delivery No.: 726DKTimes Cited: 22Cited Reference Count: 29},
	month = {Sep},
	pages = {86-90},
	type = {Article},
	abstract = {We present the 2.6. resolution crystal structure of a complex formed between G-actin and gelsolin fragment Met25-GIn160 (G1+). The structure differs from those of other gelsolin domain 1 (G1) complexes in that an additional six amino acid residues from the crucial linker region into gelsolin domain 2 (G2) are visible and are attached securely to the surface of actin. The linker segment extends away from G1 up the face of actin in a direction that infers G2 will bind along the same long-pitch helical strand as the actin bound to G1. This is consistent with a mechanism whereby G2 attaches gelsolin to the side of a filament and then directs G1 toward a position where it would disrupt actin-actin contacts. Alignment of the sequence of the structurally important residues within the G1-G2 linker with those of WH2 (WASp homology domain 2) domain protein family members (e.g. WASp (Wiscott-Aldridge syndrome protein) and thymosin beta4) suggests that the opposing activities of filament assembly and disassembly may exploit a common patch on the surface of actin. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.},
	keywords = {actin, BINDING, calcium, COMPLEX, crystal structure, DIFFRACTION DATA, F-ACTIN, FILAMENT, gelsolin, IDENTIFICATION, MODEL, MOTILITY, NUCLEATION, WH2 domain},
	isbn = {0014-5793},
	url = {<Go to ISI>://000185583000003},
	author = {Irobi, E. and Burtnick, L. D. and Urosev, D. and Narayan, K. and Robinson, R. C.}
}
@article {4646,
	title = {Domain movement in gelsolin: A calcium-activated switch},
	journal = {Science},
	volume = {286},
	number = {5446},
	year = {1999},
	note = {ISI Document Delivery No.: 261HHTimes Cited: 94Cited Reference Count: 18},
	month = {Dec},
	pages = {1939-1942},
	type = {Article},
	abstract = {The actin-binding protein gelsolin is involved in remodeling the actin cytoskeleton during growth-factor signaling, apoptosis, cytokinesis, and cell movement. Calcium-activated gelsolin severs and caps actin filaments, The 3.4 angstrom x-ray structure of the carboxyl-terminal half of gelsolin (G4-G6) in complex with actin reveals the basis for gelsolin activation. Calcium binding induces a conformational rearrangement in which domain G6 is flipped over and translated by about 40 angstroms relative to G4 and G5. The structural reorganization tears apart the continuous beta sheet core of G4 and G6. This exposes the actin-binding site on G4, enabling severing and capping of actin filaments to proceed.},
	keywords = {actin, BINDING-SITE, COMPLEX, FILAMENT, IDENTIFICATION, PLASMA GELSOLIN},
	isbn = {0036-8075},
	url = {<Go to ISI>://000084003400047},
	author = {Robinson, R. C. and Mejillano, M. and Le, V. P. and Burtnick, L. D. and Yin, H. L. and Choe, S.}
}
@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.}
}
