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| <StructureSection load='5v6h' size='340' side='right'caption='[[5v6h]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='5v6h' size='340' side='right'caption='[[5v6h]], [[Resolution|resolution]] 3.60Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5v6h]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V6H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V6H FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5v6h]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V6H FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v7b|5v7b]], [[5v6e|5v6e]], [[5v6r|5v6r]], [[5v6t|5v6t]]</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]] 3.601Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Gipc2, Semcap2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Myo6, Sv ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=5v6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v6h OCA], [https://pdbe.org/5v6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v6h RCSB], [https://www.ebi.ac.uk/pdbsum/5v6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v6h ProSAT]</span></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=5v6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v6h OCA], [http://pdbe.org/5v6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v6h RCSB], [http://www.ebi.ac.uk/pdbsum/5v6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v6h ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Disease ==
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| [[http://www.uniprot.org/uniprot/MYO6_MOUSE MYO6_MOUSE]] Note=Defects in Myo6 are the cause of Snell's waltzer, a condition characterized by circling, head-tossing, deafness and hyperactivity.
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| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/MYO6_MOUSE MYO6_MOUSE]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells. | | [https://www.uniprot.org/uniprot/GIPC2_MOUSE GIPC2_MOUSE] |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The GIPC family adaptor proteins mediate endocytosis by tethering cargo proteins to the myosin VI motor. The structural mechanisms for the GIPC/cargo and GIPC/myosin VI interactions remained unclear. PlexinD1, a transmembrane receptor that regulates neuronal and cardiovascular development, is a cargo of GIPCs. GIPC-mediated endocytic trafficking regulates PlexinD1 signaling. Here, we unravel the mechanisms of the interactions among PlexinD1, GIPCs and myosin VI by a series of crystal structures of these proteins in apo or bound states. GIPC1 forms a domain-swapped dimer in an autoinhibited conformation that hinders binding of both PlexinD1 and myosin VI. PlexinD1 binding to GIPC1 releases the autoinhibition, promoting its interaction with myosin VI. GIPCs and myosin VI interact through two distinct interfaces and form an open-ended alternating array. Our data support that this alternating array underlies the oligomerization of the GIPC/Myosin VI complexes in solution and cells.
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| Structure analyses reveal a regulated oligomerization mechanism of the PlexinD1/GIPC/myosin VI complex.,Shang G, Brautigam CA, Chen R, Lu D, Torres-Vazquez J, Zhang X Elife. 2017 May 24;6. pii: e27322. doi: 10.7554/eLife.27322. PMID:28537552<ref>PMID:28537552</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5v6h" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Myosin 3D Structures|Myosin 3D Structures]] | | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lk3 transgenic mice]] | | [[Category: Mus musculus]] |
| [[Category: Shang, G]] | | [[Category: Shang G]] |
| [[Category: Zhang, X]] | | [[Category: Zhang X]] |
| [[Category: Binding partener]]
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| [[Category: Protein binding]]
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