2OMQ

VEALYL peptide derived from human insulin chain B, residues 12-17

Summary for 2OMQ

• Entry DOI: 10.2210/pdb2omq/pdb
• Descriptor: VEALYL peptide derived from human insulin chain B, residues 12-17 (2 entities in total)
• Functional Keywords: steric zipper, anti-parallel beta-sheet, protein fibril
• Total number of polymer chains: 4
• Total formula weight: 2827.31

Authors

Ivanova, M.,Sawaya, M.R.,Eisenberg, D. (deposition date: 2007-01-22, release date: 2007-01-30, Last modification date: 2024-04-03)

Primary citation

Sawaya, M.R.,Sambashivan, S.,Nelson, R.,Ivanova, M.I.,Sievers, S.A.,Apostol, M.I.,Thompson, M.J.,Balbirnie, M.,Wiltzius, J.J.,McFarlane, H.T.,Madsen, A.,Riekel, C.,Eisenberg, D.
Atomic structures of amyloid cross-beta spines reveal varied steric zippers.
Nature, 447:453-457, 2007

PubMed Abstract: Amyloid fibrils formed from different proteins, each associated with a particular disease, contain a common cross-beta spine. The atomic architecture of a spine, from the fibril-forming segment GNNQQNY of the yeast prion protein Sup35, was recently revealed by X-ray microcrystallography. It is a pair of beta-sheets, with the facing side chains of the two sheets interdigitated in a dry 'steric zipper'. Here we report some 30 other segments from fibril-forming proteins that form amyloid-like fibrils, microcrystals, or usually both. These include segments from the Alzheimer's amyloid-beta and tau proteins, the PrP prion protein, insulin, islet amyloid polypeptide (IAPP), lysozyme, myoglobin, alpha-synuclein and beta(2)-microglobulin, suggesting that common structural features are shared by amyloid diseases at the molecular level. Structures of 13 of these microcrystals all reveal steric zippers, but with variations that expand the range of atomic architectures for amyloid-like fibrils and offer an atomic-level hypothesis for the basis of prion strains.

PubMed: 17468747
DOI: 10.1038/nature05695

Experimental method

X-RAY DIFFRACTION (2 Å)