1qjh
From Proteopedia
(New page: 200px<br /> <applet load="1qjh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qjh, resolution 2.20Å" /> '''PROTEIN AGGREGATION...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1QJH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]] with MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJH OCA]]. | + | 1QJH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]] with MG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Structure known Active Site: MG. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJH OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: ribosomal protein s6]] | [[Category: ribosomal protein s6]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:32:53 2007'' |
Revision as of 10:28, 30 October 2007
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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, ... [(full description)]
About this Structure
1QJH is a [Single protein] structure of sequence from [Thermus thermophilus] with MG as [ligand]. Structure known Active Site: MG. 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
Page seeded by OCA on Tue Oct 30 12:32:53 2007
