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1ksr
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1ksr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ksr" /> '''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-...) |
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| - | [[Image:1ksr.gif|left|200px]]<br /><applet load="1ksr" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1ksr" /> | ||
| - | '''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES'''<br /> | ||
| - | == | + | ==THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES== |
| - | The 120,000 M(r) gelation factor and alpha-actinin are among the most | + | <StructureSection load='1ksr' size='340' side='right'caption='[[1ksr]]' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1ksr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSR 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=1ksr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksr OCA], [https://pdbe.org/1ksr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksr RCSB], [https://www.ebi.ac.uk/pdbsum/1ksr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GELA_DICDI GELA_DICDI] F-actin cross-linking protein. | ||
| + | == 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/ks/1ksr_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=1ksr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 120,000 M(r) gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are rod-shaped homodimers. Each monomer chain is comprised of an actin-binding domain and a rod domain. The rod domain of the gelation factor consists of six 100-residue repetitive segments with high internal homology. We have now determined the three-dimensional structure of segment 4 of the rod domain of the gelation factor from D. discoideum using NMR spectroscopy. The segment consists of seven beta-sheets arranged in an immunoglobulin-like (Ig) fold. This is completely different from the alpha-actinin rod domain which consists of four spectrin-like alpha-helical segments. The gelation factor is the first example of an Ig-fold found in an actin-binding protein. Two highly homologous actin-binding proteins from human with similar sequences to the gelation factor, filamin and a 280,000 M(r) actin-binding protein (ABP-280), share conserved residues that form the core of the gelation factor repetitive segment structure. Thus, the segment 4 structure should be common to this subfamily of the spectrin superfamily. The structure of segment 4 together with previously published electron microscopy data, provide an explanation for the dimerization of the whole gelation factor molecule. | ||
| - | + | The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold.,Fucini P, Renner C, Herberhold C, Noegel AA, Holak TA Nat Struct Biol. 1997 Mar;4(3):223-30. PMID:9164464<ref>PMID:9164464</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1ksr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Fucini | + | [[Category: Fucini P]] |
| - | [[Category: Herberhold | + | [[Category: Herberhold C]] |
| - | [[Category: Holak | + | [[Category: Holak TA]] |
| - | [[Category: Noegel | + | [[Category: Noegel AA]] |
| - | [[Category: Renner | + | [[Category: Renner C]] |
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Current revision
THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES
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