2Y2A: Structure Of Segment Klvffa From The Amyloid-Beta Peptide ( Ab, Residues 16-21), Alternate Polymorph I

Amyloid-beta (Abeta) aggregates are the main constituent of senile plaques, the histological hallmark of Alzheimer's disease. Abeta molecules form beta-sheet containing structures that assemble into a variety of polymorphic oligomers, protofibers, and fibers that exhibit a range of lifetimes and cellular toxicities. This polymorphic nature of Abeta has frustrated its biophysical characterization, its structural determination, and our understanding of its pathological mechanism. To elucidate Abeta polymorphism in atomic detail, we determined eight new microcrystal structures of fiber-forming segments of Abeta. These structures, all of short, self-complementing pairs of beta-sheets termed steric zippers, reveal a variety of modes of self-association of Abeta. Combining these atomic structures with previous NMR studies allows us to propose several fiber models, offering molecular models for some of the repertoire of polydisperse structures accessible to Abeta. These structures and molecular models contribute fundamental information for understanding Abeta polymorphic nature and pathogenesis.
PDB ID: 2Y2ADownload
MMDB ID: 94570
PDB Deposition Date: 2010/12/14
Updated in MMDB: 2011/10
Experimental Method:
x-ray diffraction
Resolution: 1.91  Å
Source Organism:
Similar Structures:
Biological Unit for 2Y2A: monomeric; determined by author and by software (PISA)
Molecular Components in 2Y2A
Label Count Molecule
Protein (1 molecule)
Amyloid Beta A4 Protein(Gene symbol: APP)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB