1dvq
From Proteopedia
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| - | [[Image:1dvq.gif|left|200px]] | + | [[Image:1dvq.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN''' | + | {{Structure |
| + | |PDB= 1dvq |SIZE=350|CAPTION= <scene name='initialview01'>1dvq</scene>, resolution 2.Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DVQ is a [ | + | 1DVQ 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=1DVQ OCA]. |
==Reference== | ==Reference== | ||
| - | Rational design of potent human transthyretin amyloid disease inhibitors., Klabunde T, Petrassi HM, Oza VB, Raman P, Kelly JW, Sacchettini JC, Nat Struct Biol. 2000 Apr;7(4):312-21. PMID:[http:// | + | Rational design of potent human transthyretin amyloid disease inhibitors., Klabunde T, Petrassi HM, Oza VB, Raman P, Kelly JW, Sacchettini JC, Nat Struct Biol. 2000 Apr;7(4):312-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10742177 10742177] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thyroxine transport]] | [[Category: thyroxine transport]] | ||
| - | ''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 10:45:11 2008'' |
Revision as of 08:45, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN
Contents |
Overview
The human amyloid disorders, familial amyloid polyneuropathy, familial amyloid cardiomyopathy and senile systemic amyloidosis, are caused by insoluble transthyretin (TTR) fibrils, which deposit in the peripheral nerves and heart tissue. Several nonsteroidal anti-inflammatory drugs and structurally similar compounds have been found to strongly inhibit the formation of TTR amyloid fibrils in vitro. These include flufenamic acid, diclofenac, flurbiprofen, and resveratrol. Crystal structures of the protein-drug complexes have been determined to allow detailed analyses of the protein-drug interactions that stabilize the native tetrameric conformation of TTR and inhibit the formation of amyloidogenic TTR. Using a structure-based drug design approach ortho-trifluormethylphenyl anthranilic acid and N-(meta-trifluoromethylphenyl) phenoxazine 4, 6-dicarboxylic acid have been discovered to be very potent and specific TTR fibril formation inhibitors. This research provides a rationale for a chemotherapeutic approach for the treatment of TTR-associated 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
1DVQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Rational design of potent human transthyretin amyloid disease inhibitors., Klabunde T, Petrassi HM, Oza VB, Raman P, Kelly JW, Sacchettini JC, Nat Struct Biol. 2000 Apr;7(4):312-21. PMID:10742177
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