1hz3: Difference between revisions
New page: left|200px<br /> <applet load="1hz3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hz3" /> '''ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (R... |
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[[Image:1hz3.gif|left|200px]]<br /> | [[Image:1hz3.gif|left|200px]]<br /><applet load="1hz3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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'''ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)'''<br /> | '''ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)'''<br /> | ||
==Overview== | ==Overview== | ||
The self-assembly of the soluble peptide Abeta into Alzheimer's disease | The self-assembly of the soluble peptide Abeta into Alzheimer's disease amyloid is believed to involve a conformational change. Hence the solution conformation of Abeta is of significant interest. In contrast to studies in other solvents, in water Abeta is collapsed into a compact series of loops, strands, and turns and has no alpha-helical or beta-sheet structure. Conformational stabilization is primarily attributed to van der Waals and electrostatic forces. A large conspicuous uninterrupted hydrophobic patch covers approximately 25% of the surface. The compact coil structure appears meta-stable, and because fibrillization leads to formation of intermolecular beta-sheet secondary structure, a global conformational rearrangement is highly likely. A molecular hypothesis for amyloidosis includes at least two primary driving forces, changes in solvation thermodynamics during formation of amyloid deposits and relief of internal conformational stress within the soluble precursor during formation of lower-energy amyloid fibrils. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1HZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | 1HZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HZ3 OCA]. | ||
==Reference== | ==Reference== | ||
The Alzheimer's peptide a beta adopts a collapsed coil structure in water., Zhang S, Iwata K, Lachenmann MJ, Peng JW, Li S, Stimson ER, Lu Y, Felix AM, Maggio JE, Lee JP, J Struct Biol. 2000 Jun;130(2-3):130-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10940221 10940221] | The Alzheimer's peptide a beta adopts a collapsed coil structure in water., Zhang S, Iwata K, Lachenmann MJ, Peng JW, Li S, Stimson ER, Lu Y, Felix AM, Maggio JE, Lee JP, J Struct Biol. 2000 Jun;130(2-3):130-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10940221 10940221] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Felix, A | [[Category: Felix, A M.]] | ||
[[Category: Iwata, K.]] | [[Category: Iwata, K.]] | ||
[[Category: Lachenmann, M | [[Category: Lachenmann, M J.]] | ||
[[Category: Lee, J | [[Category: Lee, J P.]] | ||
[[Category: Li, S.]] | [[Category: Li, S.]] | ||
[[Category: Lu, Y.]] | [[Category: Lu, Y.]] | ||
[[Category: Maggio, J | [[Category: Maggio, J E.]] | ||
[[Category: Peng, J | [[Category: Peng, J W.]] | ||
[[Category: Stimson, E | [[Category: Stimson, E R.]] | ||
[[Category: Zhang, S.]] | [[Category: Zhang, S.]] | ||
[[Category: collapsed coil]] | [[Category: collapsed coil]] | ||
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[[Category: hydrophobic patch]] | [[Category: hydrophobic patch]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:16 2008'' | ||
Revision as of 14:06, 21 February 2008
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ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)
OverviewOverview
The self-assembly of the soluble peptide Abeta into Alzheimer's disease amyloid is believed to involve a conformational change. Hence the solution conformation of Abeta is of significant interest. In contrast to studies in other solvents, in water Abeta is collapsed into a compact series of loops, strands, and turns and has no alpha-helical or beta-sheet structure. Conformational stabilization is primarily attributed to van der Waals and electrostatic forces. A large conspicuous uninterrupted hydrophobic patch covers approximately 25% of the surface. The compact coil structure appears meta-stable, and because fibrillization leads to formation of intermolecular beta-sheet secondary structure, a global conformational rearrangement is highly likely. A molecular hypothesis for amyloidosis includes at least two primary driving forces, changes in solvation thermodynamics during formation of amyloid deposits and relief of internal conformational stress within the soluble precursor during formation of lower-energy amyloid fibrils.
DiseaseDisease
Known diseases associated with this structure: Alzheimer disease-1, APP-related OMIM:[104760], Amyloidosis, cerebroarterial, Dutch type OMIM:[104760], Amyloidosis, cerebroarterial, Iowa type OMIM:[104760], Blood group, P system OMIM:[607922]
About this StructureAbout this Structure
1HZ3 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
The Alzheimer's peptide a beta adopts a collapsed coil structure in water., Zhang S, Iwata K, Lachenmann MJ, Peng JW, Li S, Stimson ER, Lu Y, Felix AM, Maggio JE, Lee JP, J Struct Biol. 2000 Jun;130(2-3):130-41. PMID:10940221
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