2b15

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(New page: 200px<br /> <applet load="2b15" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b15, resolution 1.7&Aring;" /> '''The crystal structur...)
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[[Image:2b15.gif|left|200px]]<br /><applet load="2b15" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2b15" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2b15, resolution 1.7&Aring;" />
caption="2b15, resolution 1.7&Aring;" />
'''The crystal structure of 2,4-dinitrophenol in complex with human transthyretin'''<br />
'''The crystal structure of 2,4-dinitrophenol in complex with human transthyretin'''<br />
==Overview==
==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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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.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2B15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 and DNF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B15 OCA].
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2B15 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=DNF:'>DNF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B15 OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Damas, A.M.]]
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[[Category: Damas, A M.]]
[[Category: Morais-de-Sa, E.]]
[[Category: Morais-de-Sa, E.]]
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[[Category: Neto-Silva, R.M.]]
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[[Category: Neto-Silva, R M.]]
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[[Category: Pereira, P.J.]]
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[[Category: Pereira, P J.]]
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[[Category: Saraiva, M.J.]]
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[[Category: Saraiva, M J.]]
[[Category: DNF]]
[[Category: DNF]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: transthyretin]]
[[Category: transthyretin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:57:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:37 2008''

Revision as of 14:34, 21 February 2008


2b15, resolution 1.7Å

Drag the structure with the mouse to rotate

The crystal structure of 2,4-dinitrophenol in complex with human transthyretin

Contents

Overview

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.

Disease

Known diseases associated with this structure: Amyloid neuropathy, familial, several allelic types OMIM:[176300], Amyloidosis, senile systemic OMIM:[176300], Carpal tunnel syndrome, familial OMIM:[176300], Dystransthyretinemic hyperthyroxinemia OMIM:[176300]

About this Structure

2B15 is a Single protein structure of sequence from Homo sapiens with and as ligands. 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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