3NYL

The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain

Replaces:  1RW6

Summary for 3NYL

• Entry DOI: 10.2210/pdb3nyl/pdb
• Related: 1RW6 3NYJ
• Descriptor: Amyloid beta (A4) protein (Peptidase nexin-II, Alzheimer disease), isoform CRA_b (2 entities in total)
• Functional Keywords: alzheimer's disease, helical hairpin, cell adhesion
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 24735.11

Authors

Ha, Y.,Hu, J.,Lee, S.,Liu, X.,Wang, Y. (deposition date: 2010-07-15, release date: 2011-07-13, Last modification date: 2024-02-21)

Primary citation

Wang, Y.,Ha, Y.
The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain.
Mol.Cell, 15:343-353, 2004

PubMed Abstract: Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits in Alzheimer's disease, is derived from an integral membrane protein precursor. The biological function of the precursor is currently unclear. Here we describe the X-ray structure of E2, the largest of the three conserved domains of the precursor. The structure of E2 consists of two coiled-coil substructures connected through a continuous helix and bears an unexpected resemblance to the spectrin family of protein structures. E2 can reversibly dimerize in the solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. Heparan sulfate proteoglycans, the putative ligand for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.

PubMed: 15304215
DOI: 10.1016/j.molcel.2004.06.037

Experimental method

X-RAY DIFFRACTION (2.8 Å)