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New page: left|200px<br /><applet load="1qfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfh, resolution 2.2Å" /> '''DIMERIZATION OF GELAT...
 
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[[Image:1qfh.jpg|left|200px]]<br /><applet load="1qfh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qfh, resolution 2.2&Aring;" />
'''DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6'''<br />


==Overview==
==DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6==
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.
<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.


==About this Structure==
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>
1QFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFH OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10467095 10467095]
</div>
<div class="pdbe-citations 1qfh" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Filamin 3D structures|Filamin 3D structures]]
*[[User:Georg Mlynek/workbench|User:Georg Mlynek/workbench]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dictyostelium discoideum]]
[[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]]
 
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