1ksr

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[[Image:1ksr.gif|left|200px]]
 
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{{Structure
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==THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES==
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|PDB= 1ksr |SIZE=350|CAPTION= <scene name='initialview01'>1ksr</scene>
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<StructureSection load='1ksr' size='340' side='right'caption='[[1ksr]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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|GENE= ABPC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum])
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<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>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ksr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksr OCA], [http://www.ebi.ac.uk/pdbsum/1ksr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ksr RCSB]</span>
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[https://www.uniprot.org/uniprot/GELA_DICDI GELA_DICDI] F-actin cross-linking protein.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/1ksr_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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 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.
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==About this Structure==
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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>
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1KSR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KSR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9164464 9164464]
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</div>
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<div class="pdbe-citations 1ksr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Dictyostelium discoideum]]
[[Category: Dictyostelium discoideum]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fucini, P.]]
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[[Category: Fucini P]]
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[[Category: Herberhold, C.]]
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[[Category: Herberhold C]]
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[[Category: Holak, T A.]]
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[[Category: Holak TA]]
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[[Category: Noegel, A A.]]
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[[Category: Noegel AA]]
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[[Category: Renner, C.]]
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[[Category: Renner C]]
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[[Category: abp-120]]
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[[Category: actin binding protein]]
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[[Category: gelation factor]]
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[[Category: immunoglobulin]]
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[[Category: structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:02 2008''
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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

PDB ID 1ksr

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