1qjh
From Proteopedia
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|PDB= 1qjh |SIZE=350|CAPTION= <scene name='initialview01'>1qjh</scene>, resolution 2.20Å | |PDB= 1qjh |SIZE=350|CAPTION= <scene name='initialview01'>1qjh</scene>, resolution 2.20Å | ||
|SITE= <scene name='pdbsite=MG:Mg+Ion+Surrounded+By+A+Cluster+Of+Water+Molecules'>MG</scene> | |SITE= <scene name='pdbsite=MG:Mg+Ion+Surrounded+By+A+Cluster+Of+Water+Molecules'>MG</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjh OCA], [http://www.ebi.ac.uk/pdbsum/1qjh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qjh RCSB]</span> | ||
}} | }} | ||
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[[Category: Oliveberg, M.]] | [[Category: Oliveberg, M.]] | ||
[[Category: Otzen, D E.]] | [[Category: Otzen, D E.]] | ||
| - | [[Category: MG]] | ||
[[Category: alzheimer disease]] | [[Category: alzheimer disease]] | ||
[[Category: oligomerization]] | [[Category: oligomerization]] | ||
[[Category: ribosomal protein s6]] | [[Category: ribosomal protein s6]] | ||
| - | ''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 23:14:33 2008'' |
Revision as of 20:14, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROTEIN AGGREGATION AND ALZHEIMER'S DISEASE. CRYSTALLOGRAPHIC ANALYSIS OF THE PHENOMENON. ENGINEERED VERSION OF THE RIBOSOMAL PROTEIN S6 USED AS A STABLE SCAFFOLD TO STUDY OLIGOMERIZATION.
Overview
Limited solubility and precipitation of amyloidogenic sequences such as the Alzheimer peptide (beta-AP) are major obstacles to a molecular understanding of protein fibrillation and deposition processes. Here we have circumvented the solubility problem by stepwise engineering a beta-AP homology into a soluble scaffold, the monomeric protein S6. The S6 construct with the highest beta-AP homology crystallizes as a tetramer that is linked by the beta-AP residues forming intermolecular antiparallel beta-sheets. This construct also shows increased coil aggregation during refolding, and a 14-mer peptide encompassing the engineered sequence forms fibrils. Mutational analysis shows that intermolecular association is linked to the overall hydrophobicity of the sticky sequence and implies the existence of "structural gatekeepers" in the wild-type protein, that is, charged side chains that prevent aggregation by interrupting contiguous stretches of hydrophobic residues in the primary sequence.
About this Structure
1QJH is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly., Otzen DE, Kristensen O, Oliveberg M, Proc Natl Acad Sci U S A. 2000 Aug 29;97(18):9907-12. PMID:10944185
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