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==Structure of the Cargo Binding Domain from Human Myosin Vb==
==Structure of the Cargo Binding Domain from Human Myosin Vb==
<StructureSection load='4j5m' size='340' side='right' caption='[[4j5m]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
<StructureSection load='4j5m' size='340' side='right'caption='[[4j5m]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4j5m]] 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=4J5M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J5M FirstGlance]. <br>
<table><tr><td colspan='2'>[[4j5m]] 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=4J5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J5M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 2.07&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5l|4j5l]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA1119, MYO5B ([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=4j5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5m OCA], [https://pdbe.org/4j5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j5m RCSB], [https://www.ebi.ac.uk/pdbsum/4j5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5m 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=4j5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5m OCA], [http://pdbe.org/4j5m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j5m RCSB], [http://www.ebi.ac.uk/pdbsum/4j5m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5m ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/MYO5B_HUMAN MYO5B_HUMAN]] Microvillous inclusion disease. The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/MYO5B_HUMAN MYO5B_HUMAN] Microvillous inclusion disease. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MYO5B_HUMAN MYO5B_HUMAN]] May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis (By similarity).<ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:21282656</ref> 
[https://www.uniprot.org/uniprot/MYO5B_HUMAN MYO5B_HUMAN] May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis (By similarity).<ref>PMID:17462998</ref> <ref>PMID:19542231</ref> <ref>PMID:21282656</ref>  
<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 4j5m" style="background-color:#fffaf0;"></div>


==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: Vollmar, M]]
[[Category: Vollmar M]]
[[Category: Human myosin vb]]
[[Category: Von Delft F]]
[[Category: Intracellular traffic]]
[[Category: Organelle]]
[[Category: Protein transport]]
[[Category: Vesicle]]

Latest revision as of 15:01, 1 March 2024

Structure of the Cargo Binding Domain from Human Myosin VbStructure of the Cargo Binding Domain from Human Myosin Vb

Structural highlights

4j5m is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.07Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MYO5B_HUMAN Microvillous inclusion disease. The disease is caused by mutations affecting the gene represented in this entry.

Function

MYO5B_HUMAN May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis (By similarity).[1] [2] [3]

See Also

References

  1. ↑ Swiatecka-Urban A, Talebian L, Kanno E, Moreau-Marquis S, Coutermarsh B, Hansen K, Karlson KH, Barnaby R, Cheney RE, Langford GM, Fukuda M, Stanton BA. Myosin Vb is required for trafficking of the cystic fibrosis transmembrane conductance regulator in Rab11a-specific apical recycling endosomes in polarized human airway epithelial cells. J Biol Chem. 2007 Aug 10;282(32):23725-36. Epub 2007 Apr 26. PMID:17462998 doi:10.1074/jbc.M608531200
  2. ↑ Chu BB, Ge L, Xie C, Zhao Y, Miao HH, Wang J, Li BL, Song BL. Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-regulated translocation of NPC1L1 to the cell surface. J Biol Chem. 2009 Aug 14;284(33):22481-90. doi: 10.1074/jbc.M109.034355. Epub, 2009 Jun 19. PMID:19542231 doi:10.1074/jbc.M109.034355
  3. ↑ Roland JT, Bryant DM, Datta A, Itzen A, Mostov KE, Goldenring JR. Rab GTPase-Myo5B complexes control membrane recycling and epithelial polarization. Proc Natl Acad Sci U S A. 2011 Feb 15;108(7):2789-94. doi:, 10.1073/pnas.1010754108. Epub 2011 Jan 31. PMID:21282656 doi:10.1073/pnas.1010754108

4j5m, resolution 2.07Å

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