1gme

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(New page: 200px<br /><applet load="1gme" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gme, resolution 2.7&Aring;" /> '''CRYSTAL STRUCTURE AND...)
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[[Image:1gme.jpg|left|200px]]<br /><applet load="1gme" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gme, resolution 2.7&Aring;" />
caption="1gme, resolution 2.7&Aring;" />
'''CRYSTAL STRUCTURE AND ASSEMBLY OF AN EUKARYOTIC SMALL HEAT SHOCK PROTEIN'''<br />
'''CRYSTAL STRUCTURE AND ASSEMBLY OF AN EUKARYOTIC SMALL HEAT SHOCK PROTEIN'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1GME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GME OCA].
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1GME is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GME OCA].
==Reference==
==Reference==
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[[Category: Triticum aestivum]]
[[Category: Triticum aestivum]]
[[Category: Basha, E.]]
[[Category: Basha, E.]]
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[[Category: Friedrich, K.L.]]
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[[Category: Friedrich, K L.]]
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[[Category: Montfort, R.L.M.Van.]]
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[[Category: Montfort, R L.M Van.]]
[[Category: Slingsby, C.]]
[[Category: Slingsby, C.]]
[[Category: Vierling, E.]]
[[Category: Vierling, E.]]
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[[Category: small heat shock protein]]
[[Category: small heat shock protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:32:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:40 2008''

Revision as of 10:51, 21 February 2008


1gme, resolution 2.7Å

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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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