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| | <StructureSection load='3e2b' size='340' side='right'caption='[[3e2b]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3e2b' size='340' side='right'caption='[[3e2b]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3e2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2p1k 2p1k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3e2b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2p1k 2p1k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E2B FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2p1k|2p1k]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ctp, Cdlc1, ddlc1, CG6998 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3e2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2b OCA], [https://pdbe.org/3e2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2b RCSB], [https://www.ebi.ac.uk/pdbsum/3e2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2b ProSAT]</span></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=3e2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e2b OCA], [https://pdbe.org/3e2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e2b RCSB], [https://www.ebi.ac.uk/pdbsum/3e2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e2b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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/SWA_DROME SWA_DROME]] Has a role in localizing bicoid mRNA at the anterior margin of the oocyte during oogenesis, and a poorly characterized role in nuclear divisions in early embryogenesis.<ref>PMID:1806330</ref>
| + | [https://www.uniprot.org/uniprot/DYL1_DROME DYL1_DROME] Acts as a non-catalytic accessory component of a dynein complex (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barbar, E]] | + | [[Category: Barbar E]] |
| - | [[Category: Benison, G]] | + | [[Category: Benison G]] |
| - | [[Category: Karplus, P A]] | + | [[Category: Karplus PA]] |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Dynein]]
| + | |
| - | [[Category: Microtubule]]
| + | |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Protein-peptide complex]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
DYL1_DROME Acts as a non-catalytic accessory component of a dynein complex (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Dynein light chain LC8 is a small, dimeric, and very highly conserved globular protein that is an integral part of the dynein and myosin molecular motors but appears to have a broader role in multiple protein complexes unrelated to molecular motors. LC8 binds to two families of targets: those having a KXTQT sequence fingerprint and those having a GIQVD fingerprint. All known LC8 binding partners containing these fingerprints share a common binding site on LC8 that raises the question of what determines binding specificity. Here, we present the crystal structure of apo-LC8 at 1.7-A resolution, which, when compared with the crystal structures of several LC8 complexes, gives insight into the mechanism underlying the binding diversity of LC8. Peptide binding is associated with a shift in quaternary structure that expands the hydrophobic binding surface available to the ligand, in addition to changes in tertiary structure and ordering of LC8 around the binding groove. The observed quaternary shift suggests a mechanism by which binding at one of the two identical sites can influence binding at the other. NMR spectra of titrations with peptides from each fingerprint family show evidence of allosteric interaction between the two binding sites, to a differing degree in the two ligand families. Allosteric interaction between the binding sites may be a mechanism to promote simultaneous binding of ligands from the same family, providing a physiological role for the two fingerprints.
The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8.,Benison G, Karplus PA, Barbar E J Mol Biol. 2008 Dec 26;384(4):954-66. Epub 2008 Oct 11. PMID:18948118[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benison G, Karplus PA, Barbar E. The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8. J Mol Biol. 2008 Dec 26;384(4):954-66. Epub 2008 Oct 11. PMID:18948118 doi:10.1016/j.jmb.2008.09.083
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