2ega: Difference between revisions

Latest revision as of 18:50, 29 May 2024

Solution structure of the first SH3 domain from human KIAA0418 protein

Structural highlights

2ega is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.1016/j.ejcb.2010.05.007

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1074/jbc.M300267200

[2] 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:https://dx.doi.org/10.1016/j.ccr.2005.01.006

[3] 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:https://dx.doi.org/10.1073/pnas.0408237102

[4] 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:https://dx.doi.org/10.1126/scisignal.2000370

[5] 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:https://dx.doi.org/10.1016/j.ejcb.2010.05.007

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@@ Line 1: / Line 1: @@
-[[Image:2ega.jpg|left|200px]]
- {{Structure
+==Solution structure of the first SH3 domain from human KIAA0418 protein==
-|PDB= 2ega |SIZE=350|CAPTION= <scene name='initialview01'>2ega</scene>
+<StructureSection load='2ega' size='340' side='right'caption='[[2ega]]' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2ega]] 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=2EGA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EGA FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-|GENE= SH3MD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ega FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ega OCA], [https://pdbe.org/2ega PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ega RCSB], [https://www.ebi.ac.uk/pdbsum/2ega PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ega ProSAT], [https://www.topsan.org/Proteins/RSGI/2ega TOPSAN]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ega FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ega OCA], [http://www.ebi.ac.uk/pdbsum/2ega PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ega RCSB]</span>
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
-'''Solution structure of the first SH3 domain from human KIAA0418 protein'''
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/2ega_consurf.spt"</scriptWhenChecked>
-==About this Structure==
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-EGA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EGA OCA].
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ega ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Hayashi, F.]]
+[[Category: Hayashi F]]
-[[Category: Inoue, K.]]
+[[Category: Inoue K]]
-[[Category: Kurosaki, C.]]
+[[Category: Kurosaki C]]
-[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
+[[Category: Yokoyama S]]
-[[Category: Yokoyama, S.]]
+[[Category: Yoshida M]]
-[[Category: Yoshida, M.]]
-[[Category: kiaa0418 protein]]
-[[Category: national project on protein structural and functional analyse]]
-[[Category: nppsfa]]
-[[Category: riken structural genomics/proteomics initiative]]
-[[Category: rsgi]]
-[[Category: sh3 domain]]
-[[Category: sh3 multiple domains 1]]
-[[Category: sh3md1]]
-[[Category: signaling protein]]
-[[Category: structural genomic]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:48:38 2008''

2ega: Difference between revisions

Latest revision as of 18:50, 29 May 2024

Solution structure of the first SH3 domain from human KIAA0418 protein

Structural highlights

Function

Evolutionary Conservation

References

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Proteopedia Page Contributors and Editors (what is this?)

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