1hz3
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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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