1zcr
From Proteopedia
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| - | [[Image:1zcr.gif|left|200px]] | + | [[Image:1zcr.gif|left|200px]] |
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| - | '''Crystal structure of human Transthyretin with bound iodide''' | + | {{Structure |
| + | |PDB= 1zcr |SIZE=350|CAPTION= <scene name='initialview01'>1zcr</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Crystal structure of human Transthyretin with bound iodide''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZCR is a [ | + | 1ZCR 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=1ZCR OCA]. |
==Reference== | ==Reference== | ||
| - | The effect of iodide and chloride on transthyretin structure and stability., Hornberg A, Hultdin UW, Olofsson A, Sauer-Eriksson AE, Biochemistry. 2005 Jul 5;44(26):9290-9. PMID:[http:// | + | The effect of iodide and chloride on transthyretin structure and stability., Hornberg A, Hultdin UW, Olofsson A, Sauer-Eriksson AE, Biochemistry. 2005 Jul 5;44(26):9290-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15981995 15981995] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ig-like fold]] | [[Category: ig-like fold]] | ||
| - | ''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 15:33:54 2008'' |
Revision as of 13:33, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of human Transthyretin with bound iodide
Contents |
Overview
Transthyretin amyloid formation occurs through a process of tetramer destabilization and partial unfolding. Small molecules, including the natural ligand thyroxine, stabilize the tetrameric form of the protein, and serve as inhibitors of amyloid formation. Crucial for TTR's ligand-binding properties are its three halogen-binding sites situated at the hormone-binding channel. In this study, we have performed a structural characterization of the binding of two halides, iodide and chloride, to TTR. Chlorides are known to shield charge repulsions at the tetrameric interface of TTR, which improve tetramer stability of the protein. Our study shows that iodides, like chlorides, provide tetramer stabilization in a concentration-dependent manner and at concentrations approximately 15-fold below that of chlorides. To elucidate binding sites of the halides, we took advantage of the anomalous scattering of iodide and used the single-wavelength anomalous dispersion (SAD) method to solve the iodide-bound TTR structure at 1.8 A resolution. The structure of chloride-bound TTR was determined at 1.9 A resolution using difference Fourier techniques. The refined structures showed iodides and chlorides bound at two of the three halogen-binding sites located at the hydrophobic channel. These sites therefore also function as halide-binding sites.
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
1ZCR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The effect of iodide and chloride on transthyretin structure and stability., Hornberg A, Hultdin UW, Olofsson A, Sauer-Eriksson AE, Biochemistry. 2005 Jul 5;44(26):9290-9. PMID:15981995
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