1d0n
From Proteopedia
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'''THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.''' | '''THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.''' | ||
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[[Category: Li, C.]] | [[Category: Li, C.]] | ||
[[Category: Robinson, R.]] | [[Category: Robinson, R.]] | ||
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| - | [[Category: | + | [[Category: Mixed alpha-beta structure]] |
| - | [[Category: | + | [[Category: Protein domain packing]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:19:01 2008'' | |
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Revision as of 10:19, 2 May 2008
THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.
Overview
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 Structure
1D0N is a Single protein structure of sequence from Equus caballus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 13:19:01 2008
