1eqy
From Proteopedia
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|PDB= 1eqy |SIZE=350|CAPTION= <scene name='initialview01'>1eqy</scene>, resolution 2.3Å | |PDB= 1eqy |SIZE=350|CAPTION= <scene name='initialview01'>1eqy</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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==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. | ||
| - | |||
| - | ==Disease== | ||
| - | 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.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: CA]] | ||
[[Category: actin]] | [[Category: actin]] | ||
[[Category: gelsolin]] | [[Category: gelsolin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''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
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| , resolution 2.3Å | |||||||
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| 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
Page seeded by OCA on Sun Mar 30 20:07:59 2008
