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2yt0
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yt0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YT0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YT0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2yt0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YT0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YT0 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yt0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yt0 RCSB], [http://www.ebi.ac.uk/pdbsum/2yt0 PDBsum], [http://www.topsan.org/Proteins/RSGI/2yt0 TOPSAN]</span></td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yt0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yt0 RCSB], [http://www.ebi.ac.uk/pdbsum/2yt0 PDBsum], [http://www.topsan.org/Proteins/RSGI/2yt0 TOPSAN]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A4_MOUSE A4_MOUSE]] Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons (By similarity). Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1.<ref>PMID:15677459</ref> Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts (By similarity).<ref>PMID:15677459</ref> The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.<ref>PMID:15677459</ref> N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) (By similarity).<ref>PMID:15677459</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Harada, T | + | [[Category: Harada, T]] |
| - | [[Category: Kigawa, T | + | [[Category: Kigawa, T]] |
| - | [[Category: Koshiba, S | + | [[Category: Koshiba, S]] |
| - | [[Category: Li, H | + | [[Category: Li, H]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Tochio, N | + | [[Category: Tochio, N]] |
| - | [[Category: Watanabe, S | + | [[Category: Watanabe, S]] |
| - | [[Category: Yokoyama, S | + | [[Category: Yokoyama, S]] |
[[Category: Amyloid precursor protein]] | [[Category: Amyloid precursor protein]] | ||
[[Category: Chimera]] | [[Category: Chimera]] | ||
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[[Category: Pid domain]] | [[Category: Pid domain]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
| - | [[Category: Riken structural genomics/proteomics initiative]] | ||
[[Category: Rsgi]] | [[Category: Rsgi]] | ||
| - | [[Category: Structural genomic]] | ||
Revision as of 02:57, 25 December 2014
Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
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