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6gzl
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Complex between the dynein light chain DYNLL1/DLC8 and a peptide from the large myelin-associated glycoprotein L-MAG== | |
| + | <StructureSection load='6gzl' size='340' side='right' caption='[[6gzl]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gzl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GZL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=6gzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gzl OCA], [http://pdbe.org/6gzl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gzl RCSB], [http://www.ebi.ac.uk/pdbsum/6gzl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gzl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DYL1_HUMAN DYL1_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.<ref>PMID:10198631</ref> <ref>PMID:15193260</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The close association of myelinated axons and their myelin sheaths involves numerous intercellular molecular interactions. For example, myelin-associated glycoprotein (MAG) mediates myelin-to-axon adhesion and signalling via molecules on the axonal surface. However, knowledge about intracellular binding partners of myelin proteins, including MAG, has remained limited. The two splice isoforms of MAG, S- and L-MAG, display distinct cytoplasmic domains and spatiotemporal expression profiles. We used yeast 2-hybrid screening to identify interaction partners of L-MAG and found the dynein light chain DYNLL1 (also termed DLC8). DYNLL1 homodimers are known to facilitate dimerization of target proteins. L-MAG and DYNLL1 associate with high affinity, as confirmed with recombinant proteins in vitro. Structural analyses of the purified complex indicate that the DYNLL1-binding segment is localized close to the L-MAG C terminus, next to the Fyn kinase Tyr phosphorylation site. The crystal structure of the complex between DYNLL1 and its binding segment on L-MAG shows 2:2 binding in a parallel arrangement, indicating a heterotetrameric complex. The homology between L-MAG and previously characterized DYNLL1-ligands is limited, and some details of binding-site interactions are unique for L-MAG. The structure of the complex between the entire L-MAG cytoplasmic domain and DYNLL1, as well as that of the the extracellular domain of MAG, were modeled based on small-angle X-ray scattering data, allowing structural insights into L-MAG interactions on both membrane surfaces. Our data imply that DYNLL1 dimerizes L-MAG, but not S-MAG, through the formation of a specific 2:2 heterotetramer. This arrangement is likely to affect, in an isoform-specific manner, the functions of MAG in adhesion and myelin-to-axon signalling. This article is protected by copyright. All rights reserved. | ||
| - | + | High-affinity heterotetramer formation between the large myelin-associated glycoprotein and the dynein light chain DYNLL1.,Myllykoski M, Eichel MA, Jung RB, Kelm S, Werner HB, Kursula P J Neurochem. 2018 Sep 27. doi: 10.1111/jnc.14598. PMID:30261098<ref>PMID:30261098</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6gzl" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Kursula, P]] | [[Category: Kursula, P]] | ||
| + | [[Category: Myllykoski, M]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Cytoplasmic domain]] | ||
| + | [[Category: Heterotetramer]] | ||
| + | [[Category: Protein binding]] | ||
Revision as of 08:15, 10 October 2018
Complex between the dynein light chain DYNLL1/DLC8 and a peptide from the large myelin-associated glycoprotein L-MAG
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