1va7: Difference between revisions

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 ==Yeast Myo3 SH3 domain, triclinic crystal form==
-<StructureSection load='1va7' size='340' side='right' caption='[[1va7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='1va7' size='340' side='right'caption='[[1va7]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1va7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VA7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1va7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VA7 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ruw|1ruw]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1va7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1va7 RCSB], [http://www.ebi.ac.uk/pdbsum/1va7 PDBsum]</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=1va7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1va7 OCA], [https://pdbe.org/1va7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1va7 RCSB], [https://www.ebi.ac.uk/pdbsum/1va7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1va7 ProSAT]</span></td></tr>
-<table>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MYO3_YEAST MYO3_YEAST] One of two redundant type-I myosins implicated in the organization of the actin cytoskeleton. Required for proper actin cytoskeleton polarization and for the internalization step in endocytosis. At the cell cortex, assembles in patch-like structures together with proteins from the actin-polymerizing machinery and promotes actin assembly. Functions redundantly with LAS17 as actin nucleation-promoting factor (NPF) for the Arp2/3 complex. Motor domain phosphorylation by PAK kinases CLA4 and STE20 promotes CDC42-regulated actin assembly. Functions together with the NPF PAN1 in late stages of endocytosis. Motor domain phosphorylation by PDK1 kinases PKH1 and PKH2, and by SGK kinases YPK1 and YPK2, promotes ligand-induced, but not constitutive endocytosis of the G protein-coupled receptor STE2.<ref>PMID:8682864</ref> <ref>PMID:8614799</ref> <ref>PMID:9388196</ref> <ref>PMID:10648568</ref> <ref>PMID:10648569</ref> <ref>PMID:12725728</ref> <ref>PMID:12808026</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/1va7_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/1va7_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1va7 ConSurf].
 <div style="clear:both"></div>
 ==See Also==
-*[[Myosin|Myosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Kursula, P.]]
+[[Category: Kursula P]]
-[[Category: Lehmann, F.]]
+[[Category: Lehmann F]]
-[[Category: Song, Y H.]]
+[[Category: Song YH]]
-[[Category: Wilmanns, M.]]
+[[Category: Wilmanns M]]
-[[Category: Contractile protein]]
-[[Category: Sh3 domain]]
-[[Category: Structural genomic]]