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1rw6
From Proteopedia
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | APP (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
human APP core domain
Contents |
Overview
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.
Disease
Known disease associated with this structure: Alzheimer disease-1, APP-related OMIM:[104760], Amyloidosis, cerebroarterial, Dutch type OMIM:[104760], Amyloidosis, cerebroarterial, Iowa type OMIM:[104760]
About this Structure
1RW6 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1RW6 with [Amyloid-beta Precursor Protein]. Full crystallographic information is available from OCA.
Reference
The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain., Wang Y, Ha Y, Mol Cell. 2004 Aug 13;15(3):343-53. PMID:15304215
Page seeded by OCA on Sun Mar 30 23:33:50 2008
