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| <StructureSection load='4qh8' size='340' side='right'caption='[[4qh8]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4qh8' size='340' side='right'caption='[[4qh8]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4qh8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QH8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qh8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QH8 FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qh7|4qh7]]</td></tr> | + | </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=4qh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qh8 OCA], [https://pdbe.org/4qh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qh8 RCSB], [https://www.ebi.ac.uk/pdbsum/4qh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qh8 ProSAT]</span></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctp, Cdlc1, ddlc1, CG6998 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
| + | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qh8 OCA], [http://pdbe.org/4qh8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qh8 RCSB], [http://www.ebi.ac.uk/pdbsum/4qh8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qh8 ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/DYL1_DROME DYL1_DROME]] Acts as a non-catalytic accessory component of a dynein complex (By similarity). | + | [https://www.uniprot.org/uniprot/DYL1_DROME DYL1_DROME] Acts as a non-catalytic accessory component of a dynein complex (By similarity). |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | |
| ==See Also== | | ==See Also== |
- | *[[Dynein|Dynein]] | + | *[[Dynein 3D structures|Dynein 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Dandulakis, M G]] | + | [[Category: Dandulakis MG]] |
- | [[Category: Romes, E R]] | + | [[Category: Romes ER]] |
- | [[Category: Slep, K C]] | + | [[Category: Slep KC]] |
- | [[Category: Slevin, L K]] | + | [[Category: Slevin LK]] |
- | [[Category: Ana2]]
| + | |
- | [[Category: Cellular]]
| + | |
- | [[Category: Lc8 fold dimer]]
| + | |
- | [[Category: Motor protein]]
| + | |
- | [[Category: Target dimerization]]
| + | |
| Structural highlights
Function
DYL1_DROME Acts as a non-catalytic accessory component of a dynein complex (By similarity).
Publication Abstract from PubMed
Centrioles play a key role in nucleating polarized microtubule networks. In actively dividing cells, centrioles establish the bipolar mitotic spindle and are essential for genomic stability. Drosophila anastral spindle-2 (Ana2) is a conserved centriole duplication factor. Although recent work has demonstrated that an Ana2-dynein light chain (LC8) centriolar complex is critical for proper spindle positioning in neuroblasts, how Ana2 and LC8 interact is yet to be established. Here we examine the Ana2-LC8 interaction and map two LC8-binding sites within the central region of Ana2, Ana2M (residues 156-251). Ana2 LC8-binding site 1 contains a signature TQT motif and robustly binds LC8 (KD of 1.1 mum), whereas site 2 contains a TQC motif and binds LC8 with lower affinity (KD of 13 mum). Both LC8-binding sites flank a predicted approximately 34-residue alpha-helix. We present two independent atomic structures of LC8 dimers in complex with Ana2 LC8-binding site 1 and site 2 peptides. The Ana2 peptides form beta-strands that extend a central composite LC8 beta-sandwich. LC8 recognizes the signature TQT motif in the first LC8 binding site of Ana2, forming extensive van der Waals contacts and hydrogen bonding with the peptide, whereas the Ana2 site 2 TQC motif forms a uniquely extended beta-strand, not observed in other dynein light chain-target complexes. Size exclusion chromatography coupled with multiangle static light scattering demonstrates that LC8 dimers bind Ana2M sites and induce Ana2 tetramerization, yielding an Ana2M4-LC88 complex. LC8-mediated Ana2 oligomerization probably enhances Ana2 avidity for centriole-binding factors and may bridge multiple factors as required during spindle positioning and centriole biogenesis.
The Mechanism of Dynein Light Chain LC8-mediated Oligomerization of the Ana2 Centriole Duplication Factor.,Slevin LK, Romes EM, Dandulakis MG, Slep KC J Biol Chem. 2014 Jul 25;289(30):20727-39. doi: 10.1074/jbc.M114.576041. Epub, 2014 Jun 11. PMID:24920673[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Slevin LK, Romes EM, Dandulakis MG, Slep KC. The Mechanism of Dynein Light Chain LC8-mediated Oligomerization of the Ana2 Centriole Duplication Factor. J Biol Chem. 2014 Jul 25;289(30):20727-39. doi: 10.1074/jbc.M114.576041. Epub, 2014 Jun 11. PMID:24920673 doi:http://dx.doi.org/10.1074/jbc.M114.576041
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