1f41
From Proteopedia
(New page: 200px<br /> <applet load="1f41" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f41, resolution 1.3Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1f41.gif|left|200px]]<br /> | + | [[Image:1f41.gif|left|200px]]<br /><applet load="1f41" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f41" size=" | + | |
caption="1f41, resolution 1.3Å" /> | caption="1f41, resolution 1.3Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN AT 1.5A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN AT 1.5A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Self-assembly of the human plasma protein transthyretin (TTR) into | + | Self-assembly of the human plasma protein transthyretin (TTR) into unbranched insoluble amyloid fibrils occurs as a result of point mutations that destabilize the molecule, leading to conformational changes. The tertiary structure of native soluble TTR and many of its disease-causing mutants have been determined. Several independent studies by X-ray crystallography have suggested structural differences between TTR variants which are claimed to be of significance for amyloid formation. As these changes are minor and not consistent between the studies, we have compared all TTR structures available at the protein data bank including three wild-types, three non-amyloidogenic mutants, seven amyloidogenic mutants and nine complexes. The reference for this study is a new 1.5 A resolution structure of human wild-type TTR refined to an R-factor/R-free of 18.6 %/21.6 %. The present findings are discussed in the light of the previous structural studies of TTR variants, and show the reported structural differences to be non-significant. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F41 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:// | + | 1F41 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=1F41 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: greek key beta barrel]] | [[Category: greek key beta barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:34 2008'' |
Revision as of 10:34, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN AT 1.5A RESOLUTION
Contents |
Overview
Self-assembly of the human plasma protein transthyretin (TTR) into unbranched insoluble amyloid fibrils occurs as a result of point mutations that destabilize the molecule, leading to conformational changes. The tertiary structure of native soluble TTR and many of its disease-causing mutants have been determined. Several independent studies by X-ray crystallography have suggested structural differences between TTR variants which are claimed to be of significance for amyloid formation. As these changes are minor and not consistent between the studies, we have compared all TTR structures available at the protein data bank including three wild-types, three non-amyloidogenic mutants, seven amyloidogenic mutants and nine complexes. The reference for this study is a new 1.5 A resolution structure of human wild-type TTR refined to an R-factor/R-free of 18.6 %/21.6 %. The present findings are discussed in the light of the previous structural studies of TTR variants, and show the reported structural differences to be non-significant.
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
1F41 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin., Hornberg A, Eneqvist T, Olofsson A, Lundgren E, Sauer-Eriksson AE, J Mol Biol. 2000 Sep 22;302(3):649-69. PMID:10986125
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