@article {1368,
	title = {Calcium ion exchange in crystalline gelsolin},
	journal = {Journal of Molecular Biology},
	volume = {357},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 030IYTimes Cited: 6Cited Reference Count: 24},
	month = {Mar},
	pages = {773-782},
	type = {Article},
	abstract = {Gelsolin is a calcium and pH-sensitive modulator of actin filament length. Here, we use X-ray crystallography to examine the extraction and exchange of calcium ions from their binding sites in different crystalline forms of the activated N and C-terminal halves of gelsolin, G1-G3 and G4-G6, respectively. We demonstrate that the combination of calcium and low pH activating conditions do not induce conformational changes in G4-G6 beyond those elicited by calcium alone. EGTA is able to remove calcium ions bound to the type I and type II metal ion-binding sites in G4-G6. Constrained by crystal contacts and stabilized by interdomain interaction surfaces, the gross structure of calcium-depleted G4-G6 remains that of the activated form. However, high-resolution details of changes in the ion-binding sites may represent the initial steps toward restoration of the arrangement of domains found in the calcium-free inactive form of gelsolin in solution. Furthermore, bathing crystals with the trivalent calcium ion mimic, Tb3+, results in anomalous scattering data that permit unequivocal localization of terbium ions in each of the proposed type I and type II ion-binding sites of both halves of gelsolin. In contrast to predictions based on solution studies, we find that no calcium ion is immune to exchange. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {actin, ACTIN MONOMER, ACTIVATION, apoptosis, BINDING-SITE, C-TERMINAL HALF, calcium activation, COMPLEX, CONFORMATIONAL CHANGE, DOMAINS, ELECTRON-DENSITY MAPS, gelsolin, IDENTIFICATION, MECHANISMS, protein crystallography},
	isbn = {0022-2836},
	url = {<Go to ISI>://000236629300008},
	author = {Chumnarnsilpa, S. and Loonchanta, A. and Xue, B. and Choe, H. and Urosev, D. and Wang, H. and Lindberg, U. and Burtnick, L. D. and Robinson, R. C.}
}
@article {1612,
	title = {The structure of gelsolin bound to ATP},
	journal = {Journal of Molecular Biology},
	volume = {357},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 030IYTimes Cited: 7Cited Reference Count: 28},
	month = {Mar},
	pages = {765-772},
	type = {Article},
	abstract = {Calcium activation of the actin-modifying properties of gelsolin is sensitive to ATP. Here, we show that soaking calcium-free gelsolin crystals in ATP-containing media results in ATP occupying a site that spans the two pseudosymmetrical halves of the protein. ATP binding involves numerous polar and hydrophobic contacts and is identical for the two copies of gelsolin related by non-crystallographic symmetry within the crystal. The gamma-phosphate of ATP participates in several charge-charge interactions consistent with the preference of gelsolin for ATP, as a binding partner, over ADP. In addition, disruption of the ATP-binding site through Ca2+ activation of gelsolin reveals why ATP binds more tightly to the inactive molecule, and suggests how the binding of ATP may modulate the sensitivity of gelsolin to calcium ions. Similarities between the ATP and PIP2 interactions with the C-terminal half of gelsolin are evident from their overlapping binding sites and in that both molecules bind more tightly in the absence of calcium ions. We propose a model for how PIP2 may bind to calcium-free gelsolin based on the ATP-binding site. (c) 2006 Elsevier Ltd. All rights reserved.},
	keywords = {5-BISPHOSPHATE, actin, ATP, BINDING-SITE, calcium, CRYSTAL-STRUCTURE, DOMAIN, gelsolin, HUMAN-PLASMA GELSOLIN, IDENTIFICATION, PHOSPHATIDYLINOSITOL 4, PIP2, PROTEIN, TERMINAL HALF},
	isbn = {0022-2836},
	url = {<Go to ISI>://000236629300007},
	author = {Urosev, D. and Ma, Q. and Tan, A. L. C. and Robinson, R. C. and Burtnick, L. D.}
}
@article {813,
	title = {Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF},
	journal = {Embo Journal},
	volume = {23},
	number = {14},
	year = {2004},
	note = {ISI Document Delivery No.: 847NBTimes Cited: 41Cited Reference Count: 59},
	month = {Jul},
	pages = {2713-2722},
	type = {Article},
	abstract = {The actin filament-severing functionality of gelsolin resides in its N-terminal three domains (G1 - G3). We have determined the structure of this fragment in complex with an actin monomer. The structure reveals the dramatic domain rearrangements that activate G1 - G3, which include the replacement of interdomain interactions observed in the inactive, calcium-free protein by new contacts to actin, and by a novel G2 - G3 interface. Together, these conformational changes are critical for actin filament severing, and we suggest that their absence leads to the disease Finnish-type familial amyloidosis. Furthermore, we propose that association with actin drives the calcium-independent activation of isolated G1 G3 during apoptosis, and that a similar mechanism operates to activate native gelsolin at micromolar levels of calcium. This is the first structure of a filament-binding protein bound to actin and it sets stringent, high-resolution limitations on the arrangement of actin protomers within the filament.},
	keywords = {5-BISPHOSPHATE, actin, AMYLOIDOSIS-FINNISH TYPE, apoptosis, BINDING-SITE, CA2+ REGULATION, calcium, CRYSTAL-STRUCTURE, crystallographic structure, F-ACTIN, FAMILIAL AMYLOIDOSIS, FILAMENT BARBED ENDS, gelsolin, PHOSPHATIDYLINOSITOL 4, PLASMA GELSOLIN, X-RAY},
	isbn = {0261-4189},
	url = {<Go to ISI>://000223398800002},
	author = {Burtnick, L. D. and Urosev, D. and Irobi, E. and Narayan, K. and Robinson, R. C.}
}
@article {4661,
	title = {Cationic iron(III) complex with a hexadentate N-2,N {\textquoteright}(2),O-2-aminopyridylphenolate ligand},
	journal = {Canadian Journal of Chemistry-Revue Canadienne De Chimie},
	volume = {77},
	number = {12},
	year = {1999},
	note = {ISI Document Delivery No.: 262KYTimes Cited: 14Cited Reference Count: 34},
	month = {Dec},
	pages = {2033-2038},
	type = {Article},
	abstract = {{Iron(III) complexation with potentially hexadentate H(2)bbpen (N,N{\textquoteright}-bis(2-hydroxybenzyl)-N,N{\textquoteright}-bis(2-methylpyridyl)ethylenediamine) was studied. The resulting monocationic complex, [Fe(bbpen)](+) as its NO3- and PF6- salts, was characterized by infrared spectroscopy, mass spectrometry, elemental analyses, cyclic voltammetry, and X-ray crystallographic analysis. Crystals of [Fe(bbpen)]NO3. CH3OH are monoclinic, space group P2(1)/c},
	keywords = {ANALOGS, BINDING-SITE, CATIONIC, CRYSTAL-STRUCTURE, gallium, hexadentate, indium, iron( III), LACTOFERRIN, MODEL, OXO, phenolate, PROTEINS, pyridyl},
	isbn = {0008-4042},
	url = {<Go to ISI>://000084067500004},
	author = {Setyawati, I. A. and Rettig, S. J. and Orvig, Chris}
}
@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.}
}
