4j5l

From Proteopedia

(Difference between revisions)

Revision as of 06:11, 5 August 2016

Structure of the Cargo Binding Domain from Human Myosin Va

Structural highlights

4j5l is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4j5m
Gene:	MYH12, MYO5A (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[MYO5A_HUMAN] Griscelli disease type 3;Neuroectodermal melanolysosomal disease;Griscelli disease type 1. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[MYO5A_HUMAN] Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mehta AD, Rock RS, Rief M, Spudich JA, Mooseker MS, Cheney RE. Myosin-V is a processive actin-based motor. Nature. 1999 Aug 5;400(6744):590-3. PMID:10448864 doi:http://dx.doi.org/10.1038/23072
↑ 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

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4j5l"

@@ Line 1: / Line 1: @@
 ==Structure of the Cargo Binding Domain from Human Myosin Va==
 <StructureSection load='4j5l' size='340' side='right' caption='[[4j5l]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j5m|4j5m]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYH12, MYO5A ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j5l RCSB], [http://www.ebi.ac.uk/pdbsum/4j5l PDBsum]</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=4j5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j5l OCA], [http://pdbe.org/4j5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j5l RCSB], [http://www.ebi.ac.uk/pdbsum/4j5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j5l ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 20: / Line 21: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4j5l" style="background-color:#fffaf0;"></div>
 ==See Also==

4j5l

From Proteopedia

Revision as of 06:11, 5 August 2016

Structure of the Cargo Binding Domain from Human Myosin Va

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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