1d0n
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THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.
OverviewOverview
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).
About this StructureAbout this Structure
1D0N is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of plasma gelsolin: implications for actin severing, capping, and nucleation., Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ, Robinson RC, Cell. 1997 Aug 22;90(4):661-70. PMID:9288746
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