1tkn
From Proteopedia
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| - | [[Image:1tkn.jpg|left|200px]] | + | [[Image:1tkn.jpg|left|200px]] |
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| - | '''Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein''' | + | {{Structure |
| + | |PDB= 1tkn |SIZE=350|CAPTION= <scene name='initialview01'>1tkn</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= APP, A4, AD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TKN is a [ | + | 1TKN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15274612 15274612] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alzheimer's disease]] | [[Category: alzheimer's disease]] | ||
[[Category: app]] | [[Category: app]] | ||
| - | [[Category: four alpha- | + | [[Category: four alpha-helice]] |
[[Category: three-helical bundle]] | [[Category: three-helical bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:19:39 2008'' |
Revision as of 12:19, 20 March 2008
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| Gene: | APP, A4, AD1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 14:19:39 2008
