1HZ3

ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)

Summary for 1HZ3

• Entry DOI: 10.2210/pdb1hz3/pdb
• Descriptor: A-BETA AMYLOID (1 entity in total)
• Functional Keywords: collapsed coil, hydrophobic cluster, hydrophobic patch, sugar binding protein
• Cellular location: Membrane; Single-pass type I membrane protein: P05067
• Total number of polymer chains: 1
• Total formula weight: 2907.34

Authors

Zhang, S.,Iwata, K.,Lachenmann, M.J.,Peng, J.W.,Li, S.,Stimson, E.R.,Lu, Y.,Felix, A.M.,Maggio, J.E.,Lee, J.P. (deposition date: 2001-01-23, release date: 2001-01-31, Last modification date: 2024-05-22)

Primary citation

Zhang, S.,Iwata, K.,Lachenmann, M.J.,Peng, J.W.,Li, S.,Stimson, E.R.,Lu, Y.,Felix, A.M.,Maggio, J.E.,Lee, J.P.
The Alzheimer's peptide a beta adopts a collapsed coil structure in water.
J.Struct.Biol., 130:130-141, 2000

PubMed Abstract: 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.

PubMed: 10940221
DOI: 10.1006/jsbi.2000.4288

Experimental method

SOLUTION NMR