1TKN

Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein

Summary for 1TKN

• Entry DOI: 10.2210/pdb1tkn/pdb
• NMR Information: BMRB: 6236
• Descriptor: Amyloid beta A4 protein (1 entity in total)
• Functional Keywords: four alpha-helices, three-helical bundle, app, alzheimer's disease, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P05067
• Total number of polymer chains: 1
• Total formula weight: 13155.25

Authors

Dulubova, I.,Ho, A.,Huryeva, I.,Sudhof, T.C.,Rizo, J. (deposition date: 2004-06-08, release date: 2004-08-03, Last modification date: 2024-05-22)

Primary citation

Dulubova, I.,Ho, A.,Huryeva, I.,Sudhof, T.C.,Rizo, J.
Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein.
Biochemistry, 43:9583-9588, 2004

PubMed Abstract: Cleavage of amyloid-beta precursor protein (APP) by site-specific proteases generates amyloid-beta peptides (Abetas), which are thought to induce Alzheimer's disease. We have identified an independently folded extracellular domain of human APP localized proximal to the Abeta sequence, and determined the three-dimensional structure of this domain by NMR spectroscopy. The domain is composed of four alpha-helices, three of which form a tight antiparallel bundle, and constitutes the C-terminal half of the central extracellular region of APP that has been implicated in the regulation of APP cleavage. Sequence comparisons demonstrate that the domain is highly conserved among all members of the APP family, including invertebrate homologues, suggesting an important role for this region in the biological function of APP. The identification of this domain and the availability of its atomic structure will facilitate analysis of APP function and of the role of the extracellular region in the regulation of APP cleavage.

PubMed: 15274612
DOI: 10.1021/bi049041o

Experimental method

SOLUTION NMR