1acf: Difference between revisions

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 ==ACANTHAMOEBA CASTELLANII PROFILIN IB==
-<StructureSection load='1acf' size='340' side='right' caption='[[1acf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1acf' size='340' side='right'caption='[[1acf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1acf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ACF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1acf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ACF 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=1acf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1acf RCSB], [http://www.ebi.ac.uk/pdbsum/1acf PDBsum]</span></td></tr>
+</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&#8491;</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=1acf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acf OCA], [https://pdbe.org/1acf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1acf RCSB], [https://www.ebi.ac.uk/pdbsum/1acf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1acf ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRO1B_ACACA PRO1B_ACACA] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
 == 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/ac/1acf_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ac/1acf_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=1acf ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.
-X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates.,Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8636-40. PMID:8078936<ref>PMID:8078936</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Profilin 3D Structures|Profilin 3D Structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Acanthamoeba castellanii]]
-[[Category: Almo, S C]]
+[[Category: Large Structures]]
-[[Category: Fedorov, A A]]
+[[Category: Almo SC]]
-[[Category: Graupe, M H]]
+[[Category: Fedorov AA]]
-[[Category: Lattman, E E]]
+[[Category: Graupe MH]]
-[[Category: Magnus, K A]]
+[[Category: Lattman EE]]
-[[Category: Pollard, T D]]
+[[Category: Magnus KA]]
-[[Category: Actin-binding protein]]
+[[Category: Pollard TD]]
-[[Category: Contractile protein]]
-[[Category: Profilin]]
-[[Category: Protein binding]]