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1eqy

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|PDB= 1eqy |SIZE=350|CAPTION= <scene name='initialview01'>1eqy</scene>, resolution 2.3&Aring;
|PDB= 1eqy |SIZE=350|CAPTION= <scene name='initialview01'>1eqy</scene>, resolution 2.3&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>
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|LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5&#39;-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eqy OCA], [http://www.ebi.ac.uk/pdbsum/1eqy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eqy RCSB]</span>
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}}
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==Overview==
==Overview==
The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in a cleft between actin domains. On the actin filament model it binds tangentially, disrupting only those contacts between adjacent subunits in one helical strand. The segment 1 fold is general for all segments of the gelsolin family because the conserved residues form the core of the structure. It also provides a basis for understanding the origin of an amyloidosis caused by a gelsolin variant.
The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in a cleft between actin domains. On the actin filament model it binds tangentially, disrupting only those contacts between adjacent subunits in one helical strand. The segment 1 fold is general for all segments of the gelsolin family because the conserved residues form the core of the structure. It also provides a basis for understanding the origin of an amyloidosis caused by a gelsolin variant.
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==Disease==
 
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Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=137350 137350]]
 
==About this Structure==
==About this Structure==
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[[Category: McLaughlin, P J.]]
[[Category: McLaughlin, P J.]]
[[Category: Weeds, A G.]]
[[Category: Weeds, A G.]]
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[[Category: ATP]]
 
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[[Category: CA]]
 
[[Category: actin]]
[[Category: actin]]
[[Category: gelsolin]]
[[Category: gelsolin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:41:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:59 2008''

Revision as of 17:08, 30 March 2008


PDB ID 1eqy

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1


Overview

The structure of the segment 1 domain of gelsolin, a protein that fragments actin filaments in cells, is reported in complex with actin. Segment 1 binds monomer using an apolar patch rimmed by hydrogen bonds in a cleft between actin domains. On the actin filament model it binds tangentially, disrupting only those contacts between adjacent subunits in one helical strand. The segment 1 fold is general for all segments of the gelsolin family because the conserved residues form the core of the structure. It also provides a basis for understanding the origin of an amyloidosis caused by a gelsolin variant.

About this Structure

1EQY is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Structure of gelsolin segment 1-actin complex and the mechanism of filament severing., McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG, Nature. 1993 Aug 19;364(6439):685-92. PMID:8395021

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