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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]] 2.95&Aring;' scene=''>
<StructureSection load='4l8t' size='340' side='right'caption='[[4l8t]], [[Resolution|resolution]] 2.95&Aring;' 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</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>
<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='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;">
== 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<ref>PMID:24097982</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4l8t" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myosin|Myosin]]
*[[Myosin 3D Structures|Myosin 3D Structures]]
== 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]]
[[Category: Vesicle]]
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