5v6e: Difference between revisions
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==Crystal structure of Myosin VI in complex with GH2 domain of GIPC1== | ==Crystal structure of Myosin VI in complex with GH2 domain of GIPC1== | ||
<StructureSection load='5v6e' size='340' side='right' caption='[[5v6e]], [[Resolution|resolution]] 3.51Å' scene=''> | <StructureSection load='5v6e' size='340' side='right'caption='[[5v6e]], [[Resolution|resolution]] 3.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5v6e]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V6E OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5v6e]] 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=5V6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V6E FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.506Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5v6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v6e OCA], [https://pdbe.org/5v6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v6e RCSB], [https://www.ebi.ac.uk/pdbsum/5v6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v6e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GIPC1_MOUSE GIPC1_MOUSE] Inhibits endothelial cell migration (in vitro). May be involved in G protein-linked signaling (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== | ||
*[[Myosin|Myosin]] | *[[Myosin 3D Structures|Myosin 3D Structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Shang G]] | ||
[[Category: | [[Category: Zhang X]] | ||
Latest revision as of 16:42, 4 October 2023
Crystal structure of Myosin VI in complex with GH2 domain of GIPC1Crystal structure of Myosin VI in complex with GH2 domain of GIPC1
Structural highlights
FunctionGIPC1_MOUSE Inhibits endothelial cell migration (in vitro). May be involved in G protein-linked signaling (By similarity). Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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