1ksr: Difference between revisions

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-{{Seed}}
-[[Image:1ksr.png|left|200px]]
-<!--
+==THE REPEATING SEGMENTS OF THE F-ACTIN CROSS-LINKING GELATION FACTOR (ABP-120) HAVE AN IMMUNOGLOBULIN FOLD, NMR, 20 STRUCTURES==
-The line below this paragraph, containing "STRUCTURE_1ksr", creates the "Structure Box" on the page.
+<StructureSection load='1ksr' size='340' side='right'caption='[[1ksr]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1ksr|  PDB=1ksr  |  SCENE=  }}
+</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 FOLD, NMR, 20 STRUCTURES===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_9164464}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ksr" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9164464 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9164464}}
+__TOC__
+</StructureSection>
-==About this Structure==
-KSR is a [[Single protein]] structure of sequence from [http://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].
-==Reference==
-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]
 [[Category: Dictyostelium discoideum]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Fucini, P.]]
+[[Category: Fucini P]]
-[[Category: Herberhold, C.]]
+[[Category: Herberhold C]]
-[[Category: Holak, T A.]]
+[[Category: Holak TA]]
-[[Category: Noegel, A A.]]
+[[Category: Noegel AA]]
-[[Category: Renner, C.]]
+[[Category: Renner C]]
-[[Category: Abp-120]]
-[[Category: Actin binding protein]]
-[[Category: Gelation factor]]
-[[Category: Immunoglobulin]]
-[[Category: Structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 10:55:12 2008''