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000207434 0247_ $$2doi$$a10.1371/journal.pone.0097654
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000207434 1001_ $$0P:(DE-HGF)0$$aCsernoch, Laszlo$$b0$$eCorresponding Author
000207434 245__ $$aThe C-Terminal Random Coil Region Tunes the $\mathrm{Ca^{2+}}$-Binding Affinity of S100A4 through Conformational Activation
000207434 260__ $$aLawrence, Kan.$$bPLoS$$c2014
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000207434 520__ $$aS100A4 interacts with many binding partners upon Ca2+ activation and is strongly associated with increased metastasis formation. In order to understand the role of the C-terminal random coil for the protein function we examined how small angle X-ray scattering of the wild-type S100A4 and its C-terminal deletion mutant (residues 1–88, Δ13) changes upon Ca2+ binding. We found that the scattering intensity of wild-type S100A4 changes substantially in the 0.15–0.25 Å−1 q-range whereas a similar change is not visible in the C-terminus deleted mutant. Ensemble optimization SAXS modeling indicates that the entire C-terminus is extended when Ca2+ is bound. Pulsed field gradient NMR measurements provide further support as the hydrodynamic radius in the wild-type protein increases upon Ca2+ binding while the radius of Δ13 mutant does not change. Molecular dynamics simulations provide a rational explanation of the structural transition: the positively charged C-terminal residues associate with the negatively charged residues of the Ca2+-free EF-hands and these interactions loosen up considerably upon Ca2+-binding. As a consequence the Δ13 mutant has increased Ca2+ affinity and is constantly loaded at Ca2+ concentration ranges typically present in cells. The activation of the entire C-terminal random coil may play a role in mediating interaction with selected partner proteins of S100A4.
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000207434 7001_ $$0P:(DE-HGF)0$$aKiss, Bence$$b1
000207434 7001_ $$0P:(DE-H253)PIP1020902$$aLundholm, Ida$$b2
000207434 7001_ $$0P:(DE-HGF)0$$aBodor, Andrea$$b3
000207434 7001_ $$0P:(DE-HGF)0$$aPetoukhov, Maxim V.$$b4
000207434 7001_ $$0P:(DE-HGF)0$$aSvergun, Dmitri I.$$b5
000207434 7001_ $$0P:(DE-HGF)0$$aNyitray, László$$b6
000207434 7001_ $$0P:(DE-H253)PIP1020897$$aKatona, Gergely$$b7
000207434 7001_ $$0P:(DE-HGF)0$$aCsernoch, Laszlo$$b8
000207434 773__ $$0PERI:(DE-600)2267670-3$$a10.1371/journal.pone.0097654$$gVol. 9, no. 5, p. e97654 -$$n5$$pe97654$$tPLoS one$$v9$$x1932-6203$$y2014
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