1g1o
From Proteopedia
(New page: 200px<br /> <applet load="1g1o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g1o, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1g1o.gif|left|200px]]<br /> | + | [[Image:1g1o.gif|left|200px]]<br /><applet load="1g1o" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1g1o, resolution 2.3Å" /> | caption="1g1o, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S'''<br /> | '''CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Transthyretin is a tetrameric plasma protein associated with two forms of | + | Transthyretin is a tetrameric plasma protein associated with two forms of amyloid disease. The structure of the highly amyloidogenic transthyretin triple mutant TTRG53S/E54D/L55S determined at 2.3 A resolution reveals a novel conformation: the beta-slip. A three-residue shift in beta strand D places Leu-58 at the position normally occupied by Leu-55 now mutated to serine. The beta-slip is best defined in two of the four monomers, where it makes new protein-protein interactions to an area normally involved in complex formation with retinol-binding protein. This interaction creates unique packing arrangements, where two protein helices combine to form a double helix in agreement with fiber diffraction and electron microscopy data. Based on these findings, a novel model for transthyretin amyloid formation is presented. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G1O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1G1O is a [http://en.wikipedia.org/wiki/Single_protein 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=1G1O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lundgren, E.]] | [[Category: Lundgren, E.]] | ||
[[Category: Olofsson, A.]] | [[Category: Olofsson, A.]] | ||
| - | [[Category: Sauer-Eriksson, A | + | [[Category: Sauer-Eriksson, A E.]] |
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: beta-slip]] | [[Category: beta-slip]] | ||
[[Category: greek key]] | [[Category: greek key]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:02 2008'' |
Revision as of 10:45, 21 February 2008
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CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S
Contents |
Overview
Transthyretin is a tetrameric plasma protein associated with two forms of amyloid disease. The structure of the highly amyloidogenic transthyretin triple mutant TTRG53S/E54D/L55S determined at 2.3 A resolution reveals a novel conformation: the beta-slip. A three-residue shift in beta strand D places Leu-58 at the position normally occupied by Leu-55 now mutated to serine. The beta-slip is best defined in two of the four monomers, where it makes new protein-protein interactions to an area normally involved in complex formation with retinol-binding protein. This interaction creates unique packing arrangements, where two protein helices combine to form a double helix in agreement with fiber diffraction and electron microscopy data. Based on these findings, a novel model for transthyretin amyloid formation is presented.
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
1G1O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The beta-slip: a novel concept in transthyretin amyloidosis., Eneqvist T, Andersson K, Olofsson A, Lundgren E, Sauer-Eriksson AE, Mol Cell. 2000 Nov;6(5):1207-18. PMID:11106758
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