1y1d: Difference between revisions

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[[Image:1y1d.gif|left|200px]]
{{Seed}}
[[Image:1y1d.png|left|200px]]


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{{STRUCTURE_1y1d|  PDB=1y1d  |  SCENE=  }}  
{{STRUCTURE_1y1d|  PDB=1y1d  |  SCENE=  }}  


'''Crystal structure of transthyretin in complex with iododiflunisal'''
===Crystal structure of transthyretin in complex with iododiflunisal===




==Overview==
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Ex vivo and in vitro studies have revealed the remarkable amyloid inhibitory potency and specificity of iododiflunisal in relation to transthyretin [Almeida, Macedo, Cardoso, Alves, Valencia, Arsequell, Planas and Saraiva (2004) Biochem. J. 381, 351-356], a protein implicated in familial amyloidotic polyneuropathy. In the present paper, the crystal structure of transthyretin complexed with this diflunisal derivative is reported, which enables a detailed analysis of the protein-ligand interactions. Iododiflunisal binds very deep in the hormone-binding channel. The iodine substituent is tightly anchored into a pocket of the binding site and the fluorine atoms provide extra hydrophobic contacts with the protein. The carboxylate substituent is involved in an electrostatic interaction with the N(zeta) of a lysine residue. Moreover, ligand-induced conformational alterations in the side chain of some residues result in the formation of new intersubunit hydrogen bonds. All these new interactions, induced by iododiflunisal, increase the stability of the tetramer impairing the formation of amyloid fibrils. The crystal structure of this complex opens perspectives for the design of more specific and effective drugs for familial amyloidotic polyneuropathy patients.
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{{ABSTRACT_PUBMED_15689188}}


==About this Structure==
==About this Structure==
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[[Category: Iododiflunisal]]
[[Category: Iododiflunisal]]
[[Category: Transthyretin]]
[[Category: Transthyretin]]
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Revision as of 10:40, 29 July 2008

File:1y1d.png

Template:STRUCTURE 1y1d

Crystal structure of transthyretin in complex with iododiflunisal

Template:ABSTRACT PUBMED 15689188

About this Structure

1Y1D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Human transthyretin in complex with iododiflunisal: structural features associated with a potent amyloid inhibitor., Gales L, Macedo-Ribeiro S, Arsequell G, Valencia G, Saraiva MJ, Damas AM, Biochem J. 2005 Jun 1;388(Pt 2):615-21. PMID:15689188

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