1yjo

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[[Image:1yjo.gif|left|200px]]
[[Image:1yjo.gif|left|200px]]
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{{Structure
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|PDB= 1yjo |SIZE=350|CAPTION= <scene name='initialview01'>1yjo</scene>, resolution 1.30&Aring;
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The line below this paragraph, containing "STRUCTURE_1yjo", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_1yjo| PDB=1yjo | SCENE= }}
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|RELATEDENTRY=[[1yjp|1YJP]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yjo OCA], [http://www.ebi.ac.uk/pdbsum/1yjo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yjo RCSB]</span>
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'''Structure of NNQQNY from yeast prion Sup35 with zinc acetate'''
'''Structure of NNQQNY from yeast prion Sup35 with zinc acetate'''
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==About this Structure==
==About this Structure==
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1YJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJO OCA].
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1YJO is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJO OCA].
==Reference==
==Reference==
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[[Category: Riekel, C.]]
[[Category: Riekel, C.]]
[[Category: Sawaya, M R.]]
[[Category: Sawaya, M R.]]
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[[Category: asparagine zipper]]
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[[Category: Asparagine zipper]]
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[[Category: glutamine zipper]]
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[[Category: Glutamine zipper]]
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[[Category: keywords beta sheet]]
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[[Category: Keywords beta sheet]]
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[[Category: steric zipper]]
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[[Category: Steric zipper]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:24:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:09:55 2008''
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Revision as of 13:24, 3 May 2008

Template:STRUCTURE 1yjo

Structure of NNQQNY from yeast prion Sup35 with zinc acetate


Overview

Numerous soluble proteins convert to insoluble amyloid-like fibrils that have common properties. Amyloid fibrils are associated with fatal diseases such as Alzheimer's, and amyloid-like fibrils can be formed in vitro. For the yeast protein Sup35, conversion to amyloid-like fibrils is associated with a transmissible infection akin to that caused by mammalian prions. A seven-residue peptide segment from Sup35 forms amyloid-like fibrils and closely related microcrystals, from which we have determined the atomic structure of the cross-beta spine. It is a double beta-sheet, with each sheet formed from parallel segments stacked in register. Side chains protruding from the two sheets form a dry, tightly self-complementing steric zipper, bonding the sheets. Within each sheet, every segment is bound to its two neighbouring segments through stacks of both backbone and side-chain hydrogen bonds. The structure illuminates the stability of amyloid fibrils, their self-seeding characteristic and their tendency to form polymorphic structures.

About this Structure

1YJO is a Single protein structure. Full crystallographic information is available from OCA.

Reference

Structure of the cross-beta spine of amyloid-like fibrils., Nelson R, Sawaya MR, Balbirnie M, Madsen AO, Riekel C, Grothe R, Eisenberg D, Nature. 2005 Jun 9;435(7043):773-8. PMID:15944695 Page seeded by OCA on Sat May 3 16:24:23 2008

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