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| | ==Structure of the Cargo Binding Domain from Human Myosin Vc== | | ==Structure of the Cargo Binding Domain from Human Myosin Vc== |
| - | <StructureSection load='4l8t' size='340' side='right' caption='[[4l8t]], [[Resolution|resolution]] 2.95Å' scene=''> | + | <StructureSection load='4l8t' size='340' side='right'caption='[[4l8t]], [[Resolution|resolution]] 2.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4l8t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L8T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4l8t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L8T FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5l|4j5l]], [[4j5m|4j5m]]</td></tr> | + | </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=4l8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l8t OCA], [https://pdbe.org/4l8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l8t RCSB], [https://www.ebi.ac.uk/pdbsum/4l8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l8t ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO5C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <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=4l8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l8t OCA], [http://pdbe.org/4l8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l8t RCSB], [http://www.ebi.ac.uk/pdbsum/4l8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l8t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYO5C_HUMAN MYO5C_HUMAN]] May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues. | + | [https://www.uniprot.org/uniprot/MYO5C_HUMAN MYO5C_HUMAN] May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues. |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Assis, L H.P]] | + | [[Category: Large Structures]] |
| - | [[Category: Berridge, G]] | + | [[Category: Assis LHP]] |
| - | [[Category: Burgess-Brown, N]] | + | [[Category: Berridge G]] |
| - | [[Category: Delft, F von]]
| + | [[Category: Burgess-Brown N]] |
| - | [[Category: Krojer, T]] | + | [[Category: Krojer T]] |
| - | [[Category: Mahajan, P]] | + | [[Category: Mahajan P]] |
| - | [[Category: Murakami, M T]] | + | [[Category: Murakami MT]] |
| - | [[Category: Nascimento, A F.Z]] | + | [[Category: Nascimento AFZ]] |
| - | [[Category: Tonoli, C C.C]] | + | [[Category: Tonoli CCC]] |
| - | [[Category: Trindade, D M]] | + | [[Category: Trindade DM]] |
| - | [[Category: C-terminal globular tail]] | + | [[Category: Von Delft F]] |
| - | [[Category: Intracellular traffic]]
| + | |
| - | [[Category: Protein transport]]
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| - | [[Category: Vesicle]]
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| Structural highlights
Function
MYO5C_HUMAN May be involved in transferrin trafficking. Likely to power actin-based membrane trafficking in many physiologically crucial tissues.
Publication Abstract from PubMed
Myosin V (MyoV) motors have been implicated in the intracellular transport of diverse cargoes including vesicles, organelles, RNA-protein complexes and regulatory proteins. Here, we have solved the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process, which is unique for the MyoVc subclass. Moreover, the cargo- and motor-binding sites were structurally assigned indicating the conservation of residues involved in the recognition of adaptors for peroxisome transport and providing high-resolution insights into motor domain (MD) inhibition by CBD. These results contribute to understanding the structural requirements for cargo transport, auto-inhibition and regulatory mechanisms in myosin V motors.
Structural insights into functional overlapping and differentiation among myosin V motors.,Nascimento AF, Trindade DM, Tonoli CC, de Giuseppe PO, Assis LH, Honorato RV, de Oliveira PS, Mahajan P, Burgess-Brown NA, von Delft F, Larson RE, Murakami MT J Biol Chem. 2013 Oct 4. PMID:24097982[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nascimento AF, Trindade DM, Tonoli CC, de Giuseppe PO, Assis LH, Honorato RV, de Oliveira PS, Mahajan P, Burgess-Brown NA, von Delft F, Larson RE, Murakami MT. Structural insights into functional overlapping and differentiation among myosin V motors. J Biol Chem. 2013 Oct 4. PMID:24097982 doi:http://dx.doi.org/10.1074/jbc.M113.507202
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