|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of the first sam domain of odin== | | ==Solution structure of the first sam domain of odin== |
| - | <StructureSection load='2lmr' size='340' side='right'caption='[[2lmr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lmr' size='340' side='right'caption='[[2lmr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LMR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lmr]] 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=2LMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LMR FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANKS1A, ANKS1, KIAA0229, ODIN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2lmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lmr OCA], [https://pdbe.org/2lmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lmr RCSB], [https://www.ebi.ac.uk/pdbsum/2lmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lmr ProSAT]</span></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=2lmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lmr OCA], [https://pdbe.org/2lmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lmr RCSB], [https://www.ebi.ac.uk/pdbsum/2lmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lmr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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 == |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leone, M]] | + | [[Category: Leone M]] |
| - | [[Category: Mercurio, F]] | + | [[Category: Mercurio F]] |
| - | [[Category: Signaling protein]]
| + | |
| 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
The EphA2 receptor plays key roles in many physiological and pathological events, including cancer. The process of receptor endocytosis and the consequent degradation have attracted attention as possible means of overcoming the negative outcomes of EphA2 in cancer cells and decreasing tumor malignancy. A recent study indicates that Sam (sterile alpha motif) domains of Odin, a member of the ANKS (ankyrin repeat and sterile alpha motif domain-containing) family of proteins, are important for the regulation of EphA2 endocytosis. Odin contains two tandem Sam domains (Odin-Sam1 and -Sam2). Herein, we report on the nuclear magnetic resonance (NMR) solution structure of Odin-Sam1; through a variety of assays (employing NMR, surface plasmon resonance, and isothermal titration calorimetry techniques), we clearly demonstrate that Odin-Sam1 binds to the Sam domain of EphA2 in the low micromolar range. NMR chemical shift perturbation experiments and molecular modeling studies point out that the two Sam domains interact with a head-to-tail topology characteristic of several Sam-Sam complexes. This binding mode is similar to that we have previously proposed for the association between the Sam domains of the lipid phosphatase Ship2 and EphA2. This work further validates structural elements relevant for the heterotypic Sam-Sam interactions of EphA2 and provides novel insights for the design of potential therapeutic compounds that can modulate receptor endocytosis.
Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor.,Mercurio FA, Marasco D, Pirone L, Pedone EM, Pellecchia M, Leone M Biochemistry. 2012 Mar 13;51(10):2136-45. Epub 2012 Mar 5. PMID:22332920[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, Marasco D, Pirone L, Pedone EM, Pellecchia M, Leone M. Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor. Biochemistry. 2012 Mar 13;51(10):2136-45. Epub 2012 Mar 5. PMID:22332920 doi:10.1021/bi300141h
|
