Title : Global structure changes associated with Ca2+ activation of full-length human plasma gelsolin.

Pub. Date : 2007 Aug 31

PMID : 17604278






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Gelsolin is a six-domain (G1-G6) protein activated by calcium via a multi-step process that involves unfolding from a compact form to a more open form in which the three actin-binding sites (on the G1, G2, and G4 subdomains) become exposed. Calcium gelsolin Homo sapiens
2 To follow the global structural changes that accompany calcium activation of gelsolin, small-angle x-ray scattering (SAXS) data were collected for full-length human plasma gelsolin at nanomolar to millimolar concentrations of free Ca2+. Calcium gelsolin Homo sapiens
3 The tightly packed architecture of calcium-free gelsolin, seen from both SAXS and x-ray crystallographic models, is already partially opened up in as low as 0.5 nM Ca2+. Calcium gelsolin Homo sapiens
4 At these higher calcium levels, the SAXS-based models provide a molecular shape that is compatible with that of the crystal structures solved for Ca2+/gelsolin C-terminal and N-terminal halves+/-monomeric G-actin. Calcium gelsolin Homo sapiens