1tkn: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1tkn.jpg|left|200px]]
[[Image:1tkn.jpg|left|200px]]


{{Structure
<!--
|PDB= 1tkn |SIZE=350|CAPTION= <scene name='initialview01'>1tkn</scene>
The line below this paragraph, containing "STRUCTURE_1tkn", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE= APP, A4, AD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
-->
|DOMAIN=
{{STRUCTURE_1tkn|  PDB=1tkn |  SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tkn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tkn OCA], [http://www.ebi.ac.uk/pdbsum/1tkn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tkn RCSB]</span>
}}


'''Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein'''
'''Solution structure of CAPPD*, an independently folded extracellular domain of human Amyloid-beta Precursor Protein'''
Line 30: Line 27:
[[Category: Rizo, J.]]
[[Category: Rizo, J.]]
[[Category: Sudhof, T C.]]
[[Category: Sudhof, T C.]]
[[Category: alzheimer's disease]]
[[Category: Alzheimer's disease]]
[[Category: app]]
[[Category: App]]
[[Category: four alpha-helice]]
[[Category: Four alpha-helice]]
[[Category: three-helical bundle]]
[[Category: Three-helical bundle]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:04:04 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:57:24 2008''

Revision as of 10:04, 3 May 2008

File:1tkn.jpg

Template:STRUCTURE 1tkn

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


OverviewOverview

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.

About this StructureAbout this Structure

1TKN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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 Sat May 3 10:04:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA