1acf: Difference between revisions
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<StructureSection load='1acf' size='340' side='right' caption='[[1acf]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1acf' size='340' side='right' caption='[[1acf]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1acf]] is a 1 chain structure. 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 [http://en.wikipedia.org/wiki/Acaca Acaca]. 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> | ||
</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://pdbe.org/1acf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1acf RCSB], [http://www.ebi.ac.uk/pdbsum/1acf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1acf ProSAT]</span></td></tr> | </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://pdbe.org/1acf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1acf RCSB], [http://www.ebi.ac.uk/pdbsum/1acf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1acf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1acf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1acf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Acaca]] | |||
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
[[Category: Fedorov, A A]] | [[Category: Fedorov, A A]] | ||
Revision as of 09:22, 29 November 2017
ACANTHAMOEBA CASTELLANII PROFILIN IBACANTHAMOEBA CASTELLANII PROFILIN IB
Structural highlights
Function[PRO1A_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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