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| | ==Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments== | | ==Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments== |
| - | <StructureSection load='7m0g' size='340' side='right'caption='[[7m0g]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='7m0g' size='340' side='right'caption='[[7m0g]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7m0g]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M0G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7m0g]] 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=7M0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M0G FirstGlance]. <br> |
| | </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=7m0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m0g OCA], [https://pdbe.org/7m0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m0g RCSB], [https://www.ebi.ac.uk/pdbsum/7m0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m0g ProSAT]</span></td></tr> | | </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=7m0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m0g OCA], [https://pdbe.org/7m0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m0g RCSB], [https://www.ebi.ac.uk/pdbsum/7m0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m0g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/COF2_HUMAN COF2_HUMAN]] Typical nemaline myopathy. The disease is caused by variants affecting the gene represented in this entry.
| + | [https://www.uniprot.org/uniprot/COF2_HUMAN COF2_HUMAN] Typical nemaline myopathy. The disease is caused by variants affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/COF2_HUMAN COF2_HUMAN]] Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 (PubMed:19752190). It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity).[UniProtKB:P45591]<ref>PMID:19752190</ref>
| + | [https://www.uniprot.org/uniprot/COF2_HUMAN COF2_HUMAN] Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 (PubMed:19752190). It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity).[UniProtKB:P45591]<ref>PMID:19752190</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kraus, J]] | + | [[Category: Kraus J]] |
| - | [[Category: Perilla, J P]] | + | [[Category: Perilla JP]] |
| - | [[Category: Polenova, T]] | + | [[Category: Polenova T]] |
| - | [[Category: Xu, C]] | + | [[Category: Xu C]] |
| - | [[Category: Actin filament binding]]
| + | |
| - | [[Category: Actin filament severing]]
| + | |
| - | [[Category: Contractile protein]]
| + | |
| - | [[Category: Cytoskeletal assembly]]
| + | |
| Structural highlights
Disease
COF2_HUMAN Typical nemaline myopathy. The disease is caused by variants affecting the gene represented in this entry.
Function
COF2_HUMAN Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 (PubMed:19752190). It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity).[UniProtKB:P45591][1]
Publication Abstract from PubMed
Actin polymerization dynamics regulated by actin-binding proteins are essential for various cellular functions. The cofilin family of proteins are potent regulators of actin severing and filament disassembly. The structural basis for cofilin-isoform-specific severing activity is poorly understood as their high-resolution structures in complex with filamentous actin (F-actin) are lacking. Here, we present the atomic-resolution structure of the muscle-tissue-specific isoform, cofilin-2 (CFL2), assembled on ADP-F-actin, determined by magic-angle-spinning (MAS) NMR spectroscopy and data-guided molecular dynamics (MD) simulations. We observe an isoform-specific conformation for CFL2. This conformation is the result of a unique network of hydrogen bonding interactions within the alpha2 helix containing the non-conserved residue, Q26. Our results indicate F-site interactions that are specific between CFL2 and ADP-F-actin, revealing mechanistic insights into isoform-dependent F-actin disassembly.
Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode.,Kraus J, Russell RW, Kudryashova E, Xu C, Katyal N, Perilla JR, Kudryashov DS, Polenova T Nat Commun. 2022 Apr 19;13(1):2114. doi: 10.1038/s41467-022-29595-9. PMID:35440100[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Papalouka V, Arvanitis DA, Vafiadaki E, Mavroidis M, Papadodima SA, Spiliopoulou CA, Kremastinos DT, Kranias EG, Sanoudou D. Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle. Mol Cell Biol. 2009 Nov;29(22):6046-58. doi: 10.1128/MCB.00654-09. Epub 2009 Sep , 14. PMID:19752190 doi:http://dx.doi.org/10.1128/MCB.00654-09
- ↑ Kraus J, Russell RW, Kudryashova E, Xu C, Katyal N, Perilla JR, Kudryashov DS, Polenova T. Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode. Nat Commun. 2022 Apr 19;13(1):2114. doi: 10.1038/s41467-022-29595-9. PMID:35440100 doi:http://dx.doi.org/10.1038/s41467-022-29595-9
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