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7m0g
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7m0g is ON HOLD Authors: Kraus, J., Polenova, T., Perilla, J.P., Xu, C. Description: Magic Angle Spinning NMR Structure of Human Cofilin-2 Assemble...) |
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments== |
| + | <StructureSection load='7m0g' size='340' side='right'caption='[[7m0g]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </table> | ||
| + | == 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. | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:35440100</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7m0g" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Perilla | + | <references/> |
| - | [[Category: Polenova | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kraus J]] | ||
| + | [[Category: Perilla JP]] | ||
| + | [[Category: Polenova T]] | ||
| + | [[Category: Xu C]] | ||
Current revision
Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments
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