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[[Image:2pg1.jpg|left|200px]]<br /><applet load="2pg1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2pg1, resolution 2.800&Aring;" />
'''Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex'''<br />


==Overview==
==Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex==
Cytoplasmic dynein is a microtubule-based motor protein complex that plays, important roles in a wide range of fundamental cellular processes, including vesicular transport, mitosis, and cell migration. A single major, form of cytoplasmic dynein associates with membranous organelles, mitotic, kinetochores, the mitotic and migratory cell cortex, centrosomes, and mRNA, complexes. The ability of cytoplasmic dynein to recognize such diverse, forms of cargo is thought to be associated with its several accessory, subunits, which reside at the base of the molecule. The dynein light, chains (LCs) LC8 and TcTex1 form a subcomplex with dynein intermediate, chains, and they also interact with numerous protein and ribonucleoprotein, partners. This observation has led to the hypothesis that these subunits, serve to tether cargo to the dynein motor. Here, we present the structure, and a thermodynamic analysis of a complex of LC8 and TcTex1 associated, with their intermediate chain scaffold. The intermediate chains, effectively block the major putative cargo binding sites within the light, chains. These data suggest that, in the dynein complex, the LCs do not, bind cargo, in apparent disagreement with a role for LCs in dynein cargo, binding interactions.
<StructureSection load='2pg1' size='340' side='right'caption='[[2pg1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2pg1]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PG1 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2pg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pg1 OCA], [https://pdbe.org/2pg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pg1 RCSB], [https://www.ebi.ac.uk/pdbsum/2pg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pg1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DYL1_DROME DYL1_DROME] Acts as a non-catalytic accessory component of a dynein complex (By similarity).
== 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/pg/2pg1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2pg1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cytoplasmic dynein is a microtubule-based motor protein complex that plays important roles in a wide range of fundamental cellular processes, including vesicular transport, mitosis, and cell migration. A single major form of cytoplasmic dynein associates with membranous organelles, mitotic kinetochores, the mitotic and migratory cell cortex, centrosomes, and mRNA complexes. The ability of cytoplasmic dynein to recognize such diverse forms of cargo is thought to be associated with its several accessory subunits, which reside at the base of the molecule. The dynein light chains (LCs) LC8 and TcTex1 form a subcomplex with dynein intermediate chains, and they also interact with numerous protein and ribonucleoprotein partners. This observation has led to the hypothesis that these subunits serve to tether cargo to the dynein motor. Here, we present the structure and a thermodynamic analysis of a complex of LC8 and TcTex1 associated with their intermediate chain scaffold. The intermediate chains effectively block the major putative cargo binding sites within the light chains. These data suggest that, in the dynein complex, the LCs do not bind cargo, in apparent disagreement with a role for LCs in dynein cargo binding interactions.


==About this Structure==
Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex.,Williams JC, Roulhac PL, Roy AG, Vallee RB, Fitzgerald MC, Hendrickson WA Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10028-33. Epub 2007 Jun 5. PMID:17551010<ref>PMID:17551010</ref>
2PG1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PG1 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural and thermodynamic characterization of a cytoplasmic dynein light chain-intermediate chain complex., Williams JC, Roulhac PL, Roy AG, Vallee RB, Fitzgerald MC, Hendrickson WA, Proc Natl Acad Sci U S A. 2007 Jun 12;104(24):10028-33. Epub 2007 Jun 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17551010 17551010]
</div>
<div class="pdbe-citations 2pg1" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Hendrickson, W.A.]]
[[Category: Hendrickson WA]]
[[Category: Williams, J.C.]]
[[Category: Williams JC]]
[[Category: SO4]]
[[Category: dynein intermediate chain]]
[[Category: dynein light chain]]
[[Category: lc8]]
[[Category: pin]]
[[Category: tctex1]]
 
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