1qjh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qjh.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qjh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qjh| PDB=1qjh | SCENE= }}
{{STRUCTURE_1qjh| PDB=1qjh | SCENE= }}
-
'''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.'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10944185}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10944185 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10944185}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Oligomerization]]
[[Category: Oligomerization]]
[[Category: Ribosomal protein s6]]
[[Category: Ribosomal protein s6]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:20:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:25:34 2008''

Revision as of 11:25, 29 July 2008

Image:1qjh.png

Template:STRUCTURE 1qjh

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.

Template:ABSTRACT PUBMED 10944185

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

Page seeded by OCA on Tue Jul 29 14:25:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qjh"
Personal tools