3b56
From Proteopedia
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| - | [[Image:3b56.jpg|left|200px]] | + | [[Image:3b56.jpg|left|200px]] |
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| - | '''Crystal structure of transthyretin in complex with 3,5-diiodosalicylic acid''' | + | {{Structure |
| + | |PDB= 3b56 |SIZE=350|CAPTION= <scene name='initialview01'>3b56</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=DIU:2-HYDROXY-3,5-DIIODO-BENZOIC ACID'>DIU</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of transthyretin in complex with 3,5-diiodosalicylic acid''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3B56 is a [ | + | 3B56 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B56 OCA]. |
==Reference== | ==Reference== | ||
| - | Iodination of salicylic acid improves its binding to transthyretin., Gales L, Almeida MR, Arsequell G, Valencia G, Saraiva MJ, Damas AM, Biochim Biophys Acta. 2007 Dec 3;. PMID:[http:// | + | Iodination of salicylic acid improves its binding to transthyretin., Gales L, Almeida MR, Arsequell G, Valencia G, Saraiva MJ, Damas AM, Biochim Biophys Acta. 2007 Dec 3;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18155178 18155178] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Gales, L.]] | [[Category: Gales, L.]] | ||
[[Category: DIU]] | [[Category: DIU]] | ||
| - | [[Category: amyloid | + | [[Category: amyloid inhibitor]] |
[[Category: disease mutation]] | [[Category: disease mutation]] | ||
[[Category: glycoprotein]] | [[Category: glycoprotein]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
[[Category: transthyretin]] | [[Category: transthyretin]] | ||
| - | [[Category: vitamin | + | [[Category: vitamin some]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:56:09 2008'' |
Revision as of 16:56, 20 March 2008
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| , resolution 1.55Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of transthyretin in complex with 3,5-diiodosalicylic acid
Overview
Transthyretin (TTR) is a plasma homotetrameric protein associated with senile systemic amyloidosis and familial amyloidotic polyneuropathy. In theses cases, TTR dissociation and misfolding induces the formation of amyloidogenic intermediates that assemble into toxic oligomeric species and lead to the formation of fibrils present in amyloid deposits. The four TTR monomers associate around a central hydrophobic channel where two thyroxine molecules can bind simultaneously. In each thyroxine binding site there are three pairs of symmetry related halogen binding pockets which can accommodate the four iodine substituents of thyroxine. A number of structurally diverse small molecules that bind to the TTR channel increasing the protein stability and thereafter inhibiting amyloid fibrillogenesis have been tested. In order to take advantage of the high propensity to interactions between iodine substituents and the TTR channel we have identified two iodinated derivatives of salicylic acid, 5-iodosalicylic acid and 3,5-diiodosalicylic acid, available commercially. We report in this paper the relative binding affinities of salicylic acid and the two iodinated derivatives and the crystal structure of TTR complexed with 3,5-diiodosalicylic acid, to elucidate the higher binding affinity of this compound towards TTR.
About this Structure
3B56 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Iodination of salicylic acid improves its binding to transthyretin., Gales L, Almeida MR, Arsequell G, Valencia G, Saraiva MJ, Damas AM, Biochim Biophys Acta. 2007 Dec 3;. PMID:18155178
Page seeded by OCA on Thu Mar 20 18:56:09 2008
