2xmf: Difference between revisions
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<StructureSection load='2xmf' size='340' side='right'caption='[[2xmf]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2xmf' size='340' side='right'caption='[[2xmf]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2xmf]] is a 1 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=2XMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XMF FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIA:OCTANE+1,8-DIAMINE'>DIA</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]] 1.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIA:OCTANE+1,8-DIAMINE'>DIA</scene></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=2xmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmf OCA], [https://pdbe.org/2xmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xmf RCSB], [https://www.ebi.ac.uk/pdbsum/2xmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmf 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=2xmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xmf OCA], [https://pdbe.org/2xmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xmf RCSB], [https://www.ebi.ac.uk/pdbsum/2xmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xmf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MYO1E_MOUSE MYO1E_MOUSE] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By similarity). Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated ve (By similarity)sicles. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity).<ref>PMID:19005011</ref> | |||
==See Also== | ==See Also== | ||
*[[Myosin 3D Structures|Myosin 3D Structures]] | *[[Myosin 3D Structures|Myosin 3D Structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Allsop | [[Category: Allsop G]] | ||
[[Category: Edwards | [[Category: Edwards T]] | ||
[[Category: Peckham | [[Category: Peckham M]] | ||
Latest revision as of 15:46, 17 January 2024
Myosin 1e SH3Myosin 1e SH3
Structural highlights
FunctionMYO1E_MOUSE Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By similarity). Involved in clathrin-mediated endocytosis and intracellular movement of clathrin-coated ve (By similarity)sicles. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14 (By similarity).[1] See AlsoReferences
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