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| | ==Structure of human Cofilin1== | | ==Structure of human Cofilin1== |
| - | <StructureSection load='4bex' size='340' side='right' caption='[[4bex]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4bex' size='340' side='right'caption='[[4bex]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bex]] is a 1 chain structure with 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=4BEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BEX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bex]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BEX 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=4bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bex OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bex RCSB], [http://www.ebi.ac.uk/pdbsum/4bex 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]] 2.8Å</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=4bex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bex OCA], [https://pdbe.org/4bex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bex RCSB], [https://www.ebi.ac.uk/pdbsum/4bex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bex ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN]] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref> | + | [https://www.uniprot.org/uniprot/COF1_HUMAN COF1_HUMAN] Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.<ref>PMID:15580268</ref> <ref>PMID:21834987</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4bex" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
| - | [[Category: Cameron, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Gabrielsen, M]] | + | [[Category: Cameron J]] |
| - | [[Category: Klejnot, M]] | + | [[Category: Gabrielsen M]] |
| - | [[Category: Kozielski, F]] | + | [[Category: Klejnot M]] |
| - | [[Category: Mleczak, A]] | + | [[Category: Kozielski F]] |
| - | [[Category: Olson, M F]] | + | [[Category: Mleczak A]] |
| - | [[Category: Pannifer, A]] | + | [[Category: Olson MF]] |
| - | [[Category: Talapatra, S K]] | + | [[Category: Pannifer A]] |
| - | [[Category: Actin-binding]]
| + | [[Category: Talapatra SK]] |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
COF1_HUMAN Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization.[1] [2]
Publication Abstract from PubMed
The actin cytoskeleton is the chassis that gives a cell its shape and structure, and supplies the power for numerous dynamic processes including motility, endocytosis, intracellular transport and division. To perform these activities, the cytoskeleton undergoes constant remodelling and reorganization. One of the major actin-remodelling families are the cofilin proteins, made up of cofilin 1, cofilin 2 and actin-depolymerizing factor (ADF), which sever aged ADP-associated actin filaments to reduce filament length and provide new potential nucleation sites. Despite the significant interest in cofilin as a central node in actin-cytoskeleton dynamics, to date the only forms of cofilin for which crystal structures have been solved are from the yeast, Chromalveolata and plant kingdoms; none have previously been reported for an animal cofilin protein. Two distinct regions in animal cofilin are significantly larger than in the forms previously crystallized, suggesting that they would be uniquely organized. Therefore, it was sought to determine the structure of human cofilin 1 by X-ray crystallography to elucidate how it could interact with and regulate dynamic actin-cytoskeletal structures. Although wild-type human cofilin 1 proved to be recalcitrant, a C147A point mutant yielded crystals that diffracted to 2.8 A resolution. These studies revealed how the actin-binding helix undergoes a conformational change that increases the number of potential hydrogen bonds available for substrate binding.
Analysis of the human cofilin 1 structure reveals conformational changes required for actin binding.,Klejnot M, Gabrielsen M, Cameron J, Mleczak A, Talapatra SK, Kozielski F, Pannifer A, Olson MF Acta Crystallogr D Biol Crystallogr. 2013 Sep 1;69(Pt 9):1780-8. doi:, 10.1107/S0907444913014418. Epub 2013 Aug 17. PMID:23999301[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gohla A, Birkenfeld J, Bokoch GM. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol. 2005 Jan;7(1):21-9. Epub 2004 Dec 5. PMID:15580268 doi:10.1038/ncb1201
- ↑ Bai SW, Herrera-Abreu MT, Rohn JL, Racine V, Tajadura V, Suryavanshi N, Bechtel S, Wiemann S, Baum B, Ridley AJ. Identification and characterization of a set of conserved and new regulators of cytoskeletal organization, cell morphology and migration. BMC Biol. 2011 Aug 11;9:54. doi: 10.1186/1741-7007-9-54. PMID:21834987 doi:10.1186/1741-7007-9-54
- ↑ Klejnot M, Gabrielsen M, Cameron J, Mleczak A, Talapatra SK, Kozielski F, Pannifer A, Olson MF. Analysis of the human cofilin 1 structure reveals conformational changes required for actin binding. Acta Crystallogr D Biol Crystallogr. 2013 Sep 1;69(Pt 9):1780-8. doi:, 10.1107/S0907444913014418. Epub 2013 Aug 17. PMID:23999301 doi:10.1107/S0907444913014418
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