4l8t

</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>

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== 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>

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== References ==

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