1gme
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gme OCA], [http://www.ebi.ac.uk/pdbsum/1gme PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gme RCSB]</span> | ||
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[[Category: small heat shock protein]] | [[Category: small heat shock protein]] | ||
| - | ''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 20:47:04 2008'' |
Revision as of 17:47, 30 March 2008
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| , resolution 2.7Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE AND ASSEMBLY OF AN EUKARYOTIC SMALL HEAT SHOCK PROTEIN
Overview
The 2.7 A structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its alpha-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the alpha-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation.
About this Structure
1GME is a Single protein structure of sequence from Triticum aestivum. Full crystallographic information is available from OCA.
Reference
Crystal structure and assembly of a eukaryotic small heat shock protein., van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E, Nat Struct Biol. 2001 Dec;8(12):1025-30. PMID:11702068
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