2v17: Difference between revisions
New page: left|200px<br /><applet load="2v17" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v17, resolution 1.65Å" /> '''STRUCTURE OF THE COM... |
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==Overview== | ==Overview== | ||
The major constituent of Alzheimer's disease paired helical filaments | The major constituent of Alzheimer's disease paired helical filaments (PHF) core is intrinsically disordered protein (IDP) tau. In spite of a considerable effort, insoluble character of PHF together with inherent physical properties of IDP tau have precluded so far reconstruction of PHF 3D structure by X-ray crystallography or NMR spectroscopy. Here we present first crystallographic study of PHF core C-terminus. Using monoclonal antibody MN423 specific to the tertiary structure of the PHF core, the in vivo PHF structure was imprinted into recombinant core PHF tau. Crystallization of the complex led to determination of the structure of the core PHF tau protein fragment 386TDHGAE391 at 1.65A resolution. Structural analysis suggests important role of the core PHF C-terminus for PHF assembly. It is reasonable to expect that this approach will help to reveal the structural principles underlying the tau protein assembly into PHF and possibly will facilitate rationale drug design for inhibition of Alzheimer neurofibrillary changes. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
X-ray structure of the PHF core C-terminus: | X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease., Sevcik J, Skrabana R, Dvorsky R, Csokova N, Iqbal K, Novak M, FEBS Lett. 2007 Dec 22;581(30):5872-8. Epub 2007 Dec 3. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18061582 18061582] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: tau protein]] | [[Category: tau protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:23 2008'' | ||
Revision as of 19:52, 21 February 2008
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STRUCTURE OF THE COMPLEX OF ANTIBODY MN423 WITH A FRAGMENT OF TAU PROTEIN
OverviewOverview
The major constituent of Alzheimer's disease paired helical filaments (PHF) core is intrinsically disordered protein (IDP) tau. In spite of a considerable effort, insoluble character of PHF together with inherent physical properties of IDP tau have precluded so far reconstruction of PHF 3D structure by X-ray crystallography or NMR spectroscopy. Here we present first crystallographic study of PHF core C-terminus. Using monoclonal antibody MN423 specific to the tertiary structure of the PHF core, the in vivo PHF structure was imprinted into recombinant core PHF tau. Crystallization of the complex led to determination of the structure of the core PHF tau protein fragment 386TDHGAE391 at 1.65A resolution. Structural analysis suggests important role of the core PHF C-terminus for PHF assembly. It is reasonable to expect that this approach will help to reveal the structural principles underlying the tau protein assembly into PHF and possibly will facilitate rationale drug design for inhibition of Alzheimer neurofibrillary changes.
About this StructureAbout this Structure
2V17 is a Single protein structure of sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease., Sevcik J, Skrabana R, Dvorsky R, Csokova N, Iqbal K, Novak M, FEBS Lett. 2007 Dec 22;581(30):5872-8. Epub 2007 Dec 3. PMID:18061582
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