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| | ==Solution structure of RSGI RUH-061, a SH3 domain from human== | | ==Solution structure of RSGI RUH-061, a SH3 domain from human== |
| - | <StructureSection load='2dnu' size='340' side='right' caption='[[2dnu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2dnu' size='340' side='right'caption='[[2dnu]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2dnu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DNU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DNU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2dnu]] 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=2DNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DNU FirstGlance]. <br> |
| - | </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=2dnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dnu OCA], [http://pdbe.org/2dnu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dnu RCSB], [http://www.ebi.ac.uk/pdbsum/2dnu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dnu ProSAT], [http://www.topsan.org/Proteins/RSGI/2dnu TOPSAN]</span></td></tr> | + | </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=2dnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dnu OCA], [https://pdbe.org/2dnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dnu RCSB], [https://www.ebi.ac.uk/pdbsum/2dnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dnu ProSAT], [https://www.topsan.org/Proteins/RSGI/2dnu TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SPD2A_HUMAN SPD2A_HUMAN]] Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide.<ref>PMID:12615925</ref> <ref>PMID:15710328</ref> <ref>PMID:15710903</ref> <ref>PMID:19755710</ref> <ref>PMID:20609497</ref> | + | [https://www.uniprot.org/uniprot/SPD2A_HUMAN SPD2A_HUMAN] Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide.<ref>PMID:12615925</ref> <ref>PMID:15710328</ref> <ref>PMID:15710903</ref> <ref>PMID:19755710</ref> <ref>PMID:20609497</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Hayashi, F]] | + | [[Category: Large Structures]] |
| - | [[Category: Hirota, H]] | + | [[Category: Hayashi F]] |
| - | [[Category: Kurosaki, C]] | + | [[Category: Hirota H]] |
| - | [[Category: Nagashima, T]] | + | [[Category: Kurosaki C]] |
| - | [[Category: Ohashi, W]] | + | [[Category: Nagashima T]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Ohashi W]] |
| - | [[Category: Yokoyama, S]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Yoshida, M]] | + | [[Category: Yoshida M]] |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Sh3]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
SPD2A_HUMAN Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. In association with ADAM12, mediates the neurotoxic effect of beta-amyloid peptide.[1] [2] [3] [4] [5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Abram CL, Seals DF, Pass I, Salinsky D, Maurer L, Roth TM, Courtneidge SA. The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells. J Biol Chem. 2003 May 9;278(19):16844-51. Epub 2003 Mar 3. PMID:12615925 doi:http://dx.doi.org/10.1074/jbc.M300267200
- ↑ Seals DF, Azucena EF Jr, Pass I, Tesfay L, Gordon R, Woodrow M, Resau JH, Courtneidge SA. The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells. Cancer Cell. 2005 Feb;7(2):155-65. PMID:15710328 doi:http://dx.doi.org/10.1016/j.ccr.2005.01.006
- ↑ Malinin NL, Wright S, Seubert P, Schenk D, Griswold-Prenner I. Amyloid-beta neurotoxicity is mediated by FISH adapter protein and ADAM12 metalloprotease activity. Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):3058-63. Epub 2005 Feb 14. PMID:15710903 doi:http://dx.doi.org/10.1073/pnas.0408237102
- ↑ Gianni D, Diaz B, Taulet N, Fowler B, Courtneidge SA, Bokoch GM. Novel p47(phox)-related organizers regulate localized NADPH oxidase 1 (Nox1) activity. Sci Signal. 2009 Sep 15;2(88):ra54. doi: 10.1126/scisignal.2000370. PMID:19755710 doi:http://dx.doi.org/10.1126/scisignal.2000370
- ↑ Gianni D, DerMardirossian C, Bokoch GM. Direct interaction between Tks proteins and the N-terminal proline-rich region (PRR) of NoxA1 mediates Nox1-dependent ROS generation. Eur J Cell Biol. 2011 Feb-Mar;90(2-3):164-71. doi: 10.1016/j.ejcb.2010.05.007., Epub 2010 Jul 6. PMID:20609497 doi:http://dx.doi.org/10.1016/j.ejcb.2010.05.007
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