1tkn
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cleavage of amyloid-beta precursor protein (APP) by site-specific | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Huryeva, I.]] | [[Category: Huryeva, I.]] | ||
[[Category: Rizo, J.]] | [[Category: Rizo, J.]] | ||
| - | [[Category: Sudhof, T | + | [[Category: Sudhof, T C.]] |
[[Category: alzheimer's disease]] | [[Category: alzheimer's disease]] | ||
[[Category: app]] | [[Category: app]] | ||
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[[Category: three-helical bundle]] | [[Category: three-helical bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:14:33 2008'' |
Revision as of 13:14, 21 February 2008
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Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Alzheimer disease-1, APP-related OMIM:[104760], Amyloidosis, cerebroarterial, Dutch type OMIM:[104760], Amyloidosis, cerebroarterial, Iowa type OMIM:[104760], Blood group, P system OMIM:[607922]
About this Structure
1TKN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein., Dulubova I, Ho A, Huryeva I, Sudhof TC, Rizo J, Biochemistry. 2004 Aug 3;43(30):9583-8. PMID:15274612
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