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| | ==NMR structure of an Odin-Sam1 stapled peptide== | | ==NMR structure of an Odin-Sam1 stapled peptide== |
| - | <StructureSection load='6f7o' size='340' side='right'caption='[[6f7o]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6f7o' size='340' side='right'caption='[[6f7o]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6f7o]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F7O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6f7o]] 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=6F7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F7O FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MK8:2-METHYL-L-NORLEUCINE'>MK8</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MK8:2-METHYL-L-NORLEUCINE'>MK8</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f7m|6f7m]], [[6f7n|6f7n]]</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=6f7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f7o OCA], [https://pdbe.org/6f7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f7o RCSB], [https://www.ebi.ac.uk/pdbsum/6f7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f7o ProSAT]</span></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=6f7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f7o OCA], [http://pdbe.org/6f7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f7o RCSB], [http://www.ebi.ac.uk/pdbsum/6f7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f7o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ANS1A_HUMAN ANS1A_HUMAN]] Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity).<ref>PMID:17875921</ref> | + | [https://www.uniprot.org/uniprot/ANS1A_HUMAN ANS1A_HUMAN] Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity).<ref>PMID:17875921</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leone, M]] | + | [[Category: Leone M]] |
| - | [[Category: Mercurio, F A]] | + | [[Category: Mercurio FA]] |
| - | [[Category: Sam domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Stapled peptide]]
| + | |
| Structural highlights
Function
ANS1A_HUMAN Regulator of different signaling pathways. Regulates EPHA8 receptor tyrosine kinase signaling to control cell migration and neurite retraction (By similarity).[1]
Publication Abstract from PubMed
Sam (Sterile alpha motif) domains represent small helical protein-protein interaction modules which play versatile functions in different cellular processes. The Sam domain from the EphA2 receptor binds the Sam domain of the lipid phosphatase Ship2 and this interaction modulates receptor endocytosis and degradation primarily generating pro-oncogenic effects in cell. To identify molecule antagonists of the EphA2-Sam/Ship2-Sam complex with anti-cancer activity, we focused on hydrocarbon helical stapled peptides. EphA2-Sam and one of its interactors (i.e., the first Sam domain of the adaptor protein Odin) were used as model systems for peptide design. Increase in helicity in the stapled peptides, with respect to the corresponding linear/native-like regions, was proved by structural studies conducted through CD (Circular Dichroism) and NMR (Nuclear Magnetic Resonance). Interestingly, interaction assays by means of NMR, SPR (Surface Plasmon Resonance) and MST (MicroScale Thermophoresis) techniques led to the discovery of a novel ligand of Ship2-Sam.
Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2.,Mercurio FA, Pirone L, Di Natale C, Marasco D, Pedone EM, Leone M Bioorg Chem. 2018 Jul 20;80:602-610. doi: 10.1016/j.bioorg.2018.07.013. PMID:30036816[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shin J, Gu C, Park E, Park S. Identification of phosphotyrosine binding domain-containing proteins as novel downstream targets of the EphA8 signaling function. Mol Cell Biol. 2007 Dec;27(23):8113-26. Epub 2007 Sep 17. PMID:17875921 doi:http://dx.doi.org/MCB.00794-07
- ↑ Mercurio FA, Pirone L, Di Natale C, Marasco D, Pedone EM, Leone M. Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2. Bioorg Chem. 2018 Jul 20;80:602-610. doi: 10.1016/j.bioorg.2018.07.013. PMID:30036816 doi:http://dx.doi.org/10.1016/j.bioorg.2018.07.013
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