1d0n
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d0n OCA], [http://www.ebi.ac.uk/pdbsum/1d0n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d0n RCSB]</span> | ||
}} | }} | ||
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[[Category: protein domain packing]] | [[Category: protein domain packing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:32:18 2008'' |
Revision as of 16:32, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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