1qfh: Difference between revisions

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-[[Image:1qfh.jpg|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1qfh", creates the "Structure Box" on the page.
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-{{STRUCTURE_1qfh|  PDB=1qfh  |  SCENE=  }}
-'''DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6'''
+==DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6==
+<StructureSection load='1qfh' size='340' side='right'caption='[[1qfh]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qfh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1qfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfh OCA], [https://pdbe.org/1qfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfh RCSB], [https://www.ebi.ac.uk/pdbsum/1qfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfh 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/qf/1qfh_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=1qfh ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 A resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of beta-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1-5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.
-==Overview==
+Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod.,McCoy AJ, Fucini P, Noegel AA, Stewart M Nat Struct Biol. 1999 Sep;6(9):836-41. PMID:10467095<ref>PMID:10467095</ref>
-Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 A resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of beta-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1-5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-QFH 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=1QFH OCA].
+</div>
+<div class="pdbe-citations 1qfh" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod., McCoy AJ, Fucini P, Noegel AA, Stewart M, Nat Struct Biol. 1999 Sep;6(9):836-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10467095 10467095]
+*[[Filamin 3D structures|Filamin 3D structures]]
+*[[User:Georg Mlynek/workbench|User:Georg Mlynek/workbench]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Dictyostelium discoideum]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Fucini, P.]]
+[[Category: Fucini P]]
-[[Category: Mccoy, A J.]]
+[[Category: Mccoy AJ]]
-[[Category: Noegel, A A.]]
+[[Category: Noegel AA]]
-[[Category: Stewart, M.]]
+[[Category: Stewart M]]
-[[Category: Abp-120]]
-[[Category: Actin binding protein]]
-[[Category: Gelation factor]]
-[[Category: Immunoglobulin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:12:21 2008''