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1d0n
From Proteopedia
(New page: 200px<br /><applet load="1d0n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d0n, resolution 2.5Å" /> '''THE CRYSTAL STRUCTURE...) |
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| - | [[Image:1d0n.jpg|left|200px]]<br /><applet load="1d0n" size=" | + | [[Image:1d0n.jpg|left|200px]]<br /><applet load="1d0n" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1d0n, resolution 2.5Å" /> | caption="1d0n, resolution 2.5Å" /> | ||
'''THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.'''<br /> | '''THE CRYSTAL STRUCTURE OF CALCIUM-FREE EQUINE PLASMA GELSOLIN.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of gelsolin has been determined by crystallography and | + | 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== | ==About this Structure== | ||
| - | 1D0N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http:// | + | 1D0N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D0N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burtnick, L | + | [[Category: Burtnick, L D.]] |
[[Category: Li, C.]] | [[Category: Li, C.]] | ||
[[Category: Robinson, R.]] | [[Category: Robinson, R.]] | ||
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[[Category: protein domain packing]] | [[Category: protein domain packing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:40 2008'' |
Revision as of 10:11, 21 February 2008
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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 Thu Feb 21 12:11:40 2008
