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| - | [[Image:2m38.jpg|left|200px]] | |
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| - | {{STRUCTURE_2m38| PDB=2m38 | SCENE= }}
| + | ==PTB domain of AIDA1== |
| | + | <StructureSection load='2m38' size='340' side='right'caption='[[2m38]]' scene=''> |
| | + | == Structural highlights == |
| | + | <table><tr><td colspan='2'>[[2m38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M38 FirstGlance]. <br> |
| | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2m38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m38 OCA], [https://pdbe.org/2m38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m38 RCSB], [https://www.ebi.ac.uk/pdbsum/2m38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m38 ProSAT]</span></td></tr> |
| | + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ANS1B_HUMAN ANS1B_HUMAN] Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity).<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.<ref>PMID:15862129</ref> <ref>PMID:15347684</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | AIDA1 links persistent chemical signaling events occurring at the neuronal synapse with global changes in gene expression. Consistent with its role as a scaffolding protein, AIDA1 is composed of several protein-protein interaction domains. Here we report the NMR structure of the carboxy terminally located phosphotyrosine binding domain (PTB) that is common to all AIDA1 splice variants. A comprehensive survey of peptides identified a consensus sequence around an NxxY motif that is shared by a number of related neuronal signaling proteins. Using peptide arrays and fluorescence based assays, we determined that the AIDA1 PTB domain binds amyloid protein precursor (APP) in a similar manner to the X11/Mint PTB domain, albeit at reduced affinity ( approximately 10 microM) that may allow AIDA1 to effectively sample APP, as well as other protein partners in a variety of cellular contexts. |
| | | | |
| - | ===PTB domain of AIDA1===
| + | Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein.,Smirnova E, Shanbhag R, Kurabi A, Mobli M, Kwan JJ, Donaldson LW PLoS One. 2013 Jun 14;8(6):e65605. doi: 10.1371/journal.pone.0065605. Print 2013. PMID:23799029<ref>PMID:23799029</ref> |
| | | | |
| - | | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | ==About this Structure== | + | </div> |
| - | [[2m38]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M38 OCA].
| + | <div class="pdbe-citations 2m38" style="background-color:#fffaf0;"></div> |
| | + | == References == |
| | + | <references/> |
| | + | __TOC__ |
| | + | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Donaldson, L.]] | + | [[Category: Large Structures]] |
| - | [[Category: Peptide binding protein]] | + | [[Category: Donaldson L]] |
| - | [[Category: Phosphotyrosine binding domain]]
| + | |
| Structural highlights
Function
ANS1B_HUMAN Isoform 2 may participate in the regulation of nucleoplasmic coilin protein interactions in neuronal and transformed cells.[1] [2] Isoform 3 can regulate global protein synthesis by altering nucleolar numbers (By similarity).[3] [4] Isoform 4 may play a role as a modulator of APP processing. Overexpression can down-regulate APP processing.[5] [6]
Publication Abstract from PubMed
AIDA1 links persistent chemical signaling events occurring at the neuronal synapse with global changes in gene expression. Consistent with its role as a scaffolding protein, AIDA1 is composed of several protein-protein interaction domains. Here we report the NMR structure of the carboxy terminally located phosphotyrosine binding domain (PTB) that is common to all AIDA1 splice variants. A comprehensive survey of peptides identified a consensus sequence around an NxxY motif that is shared by a number of related neuronal signaling proteins. Using peptide arrays and fluorescence based assays, we determined that the AIDA1 PTB domain binds amyloid protein precursor (APP) in a similar manner to the X11/Mint PTB domain, albeit at reduced affinity ( approximately 10 microM) that may allow AIDA1 to effectively sample APP, as well as other protein partners in a variety of cellular contexts.
Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein.,Smirnova E, Shanbhag R, Kurabi A, Mobli M, Kwan JJ, Donaldson LW PLoS One. 2013 Jun 14;8(6):e65605. doi: 10.1371/journal.pone.0065605. Print 2013. PMID:23799029[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu H, Hebert MD. A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC Cell Biol. 2005 Apr 29;6(1):23. PMID:15862129 doi:http://dx.doi.org/10.1186/1471-2121-6-23
- ↑ Ghersi E, Noviello C, D'Adamio L. Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J Biol Chem. 2004 Nov 19;279(47):49105-12. Epub 2004 Sep 3. PMID:15347684 doi:http://dx.doi.org/10.1074/jbc.M405329200
- ↑ Xu H, Hebert MD. A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC Cell Biol. 2005 Apr 29;6(1):23. PMID:15862129 doi:http://dx.doi.org/10.1186/1471-2121-6-23
- ↑ Ghersi E, Noviello C, D'Adamio L. Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J Biol Chem. 2004 Nov 19;279(47):49105-12. Epub 2004 Sep 3. PMID:15347684 doi:http://dx.doi.org/10.1074/jbc.M405329200
- ↑ Xu H, Hebert MD. A novel EB-1/AIDA-1 isoform, AIDA-1c, interacts with the Cajal body protein coilin. BMC Cell Biol. 2005 Apr 29;6(1):23. PMID:15862129 doi:http://dx.doi.org/10.1186/1471-2121-6-23
- ↑ Ghersi E, Noviello C, D'Adamio L. Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner. J Biol Chem. 2004 Nov 19;279(47):49105-12. Epub 2004 Sep 3. PMID:15347684 doi:http://dx.doi.org/10.1074/jbc.M405329200
- ↑ Smirnova E, Shanbhag R, Kurabi A, Mobli M, Kwan JJ, Donaldson LW. Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein. PLoS One. 2013 Jun 14;8(6):e65605. doi: 10.1371/journal.pone.0065605. Print 2013. PMID:23799029 doi:http://dx.doi.org/10.1371/journal.pone.0065605
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