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1x67
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:1x67.png|left|200px]] | ||
| - | + | ==Solution structure of the cofilin homology domain of HIP-55 (drebrin-like protein)== | |
| - | + | <StructureSection load='1x67' size='340' side='right'caption='[[1x67]]' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1x67]] 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=1X67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X67 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1x67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x67 OCA], [https://pdbe.org/1x67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x67 RCSB], [https://www.ebi.ac.uk/pdbsum/1x67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x67 ProSAT], [https://www.topsan.org/Proteins/RSGI/1x67 TOPSAN]</span></td></tr> |
| - | + | </table> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DBNL_HUMAN DBNL_HUMAN] Actin-binding adapter protein. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Its association with dynamin suggests that it may also connect the actin cytoskeleton to endocytic function. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes. Binds to F-actin but is not involved in actin polymerization, capping or bundling. Does not bind G-actin.<ref>PMID:14729663</ref> | ||
| + | == 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/x6/1x67_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/main_output.php?pdb_ID=1x67 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma. | ||
| - | + | NMR solution structures of actin depolymerizing factor homology domains.,Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801<ref>PMID:19768801</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1x67" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Goroncy | + | [[Category: Large Structures]] |
| - | [[Category: Inoue | + | [[Category: Goroncy AK]] |
| - | [[Category: Kigawa | + | [[Category: Inoue M]] |
| - | [[Category: Kobayashi | + | [[Category: Kigawa T]] |
| - | [[Category: Koshiba | + | [[Category: Kobayashi N]] |
| - | + | [[Category: Koshiba S]] | |
| - | [[Category: Sato | + | [[Category: Sato M]] |
| - | [[Category: Tochio | + | [[Category: Tochio N]] |
| - | [[Category: Yokoyama | + | [[Category: Yokoyama S]] |
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Current revision
Solution structure of the cofilin homology domain of HIP-55 (drebrin-like protein)
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Categories: Homo sapiens | Large Structures | Goroncy AK | Inoue M | Kigawa T | Kobayashi N | Koshiba S | Sato M | Tochio N | Yokoyama S

