2b14: Difference between revisions

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[[Image:2b14.gif|left|200px]]
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{{STRUCTURE_2b14|  PDB=2b14  |  SCENE=  }}  
{{STRUCTURE_2b14|  PDB=2b14  |  SCENE=  }}  


'''The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant Transthyretin Leu 55 Pro'''
===The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant Transthyretin Leu 55 Pro===




==Overview==
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Systemic deposition of transthyretin (TTR) amyloid fibrils is always observed in familial amyloidotic polyneuropathy, senile systemic amyloidosis and familial amyloidotic cardiomyopathy patients. Destabilization of the molecule leads to a cascade of events which result in fibril formation. The destabilization of a native protein with consequent conformational changes appears to be a common link in several human amyloid diseases. Intensive research has been directed towards finding small molecules that could work as therapeutic agents for the prevention/inhibition of amyloid diseases through stabilization of the native fold of the potentially amyloidogenic protein. This work provides insight into the structural determinants of the highly stabilizing effects of 2,4-dinitrophenol on wild-type TTR. It is also shown that similar interactions are established between this molecule and two highly amyloidogenic TTR variants: TTR L55P and TTR Y78F. In the three crystal complexes, 2,4-dinitrophenol occupies the two hormone-binding sites of the TTR tetramer. As a result of 2,4-dinitrophenol binding, the two dimers in the TTR tetramer become closer, increasing the stability of the protein. The three-dimensional structures now determined allow a comprehensive description of key interactions between transthyretin and 2,4-dinitrophenol, a small compound that holds promise as a template for the design of a therapeutical drug for amyloid diseases.
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{{ABSTRACT_PUBMED_16627944}}


==About this Structure==
==About this Structure==
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[[Category: Tetramer stabilizer]]
[[Category: Tetramer stabilizer]]
[[Category: Transthyretin]]
[[Category: Transthyretin]]
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Revision as of 12:19, 29 July 2008

File:2b14.png

Template:STRUCTURE 2b14

The crystal structure of 2,4-dinitrophenol in complex with the amyloidogenic variant Transthyretin Leu 55 Pro

Template:ABSTRACT PUBMED 16627944

About this Structure

2B14 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The binding of 2,4-dinitrophenol to wild-type and amyloidogenic transthyretin., Morais-de-Sa E, Neto-Silva RM, Pereira PJ, Saraiva MJ, Damas AM, Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):512-9. Epub 2006, Apr 19. PMID:16627944

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