4lnz

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(Difference between revisions)

Revision as of 17:39, 5 August 2016

Crystal structure of human Myosin 5b globular domain

Structural highlights

4lnz is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4lli
Gene:	MYO5B, KIAA1119 (HUMAN)
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]

Publication Abstract from PubMed

Vertebrate type V myosins (MyoV) Myo5a, Myo5b, and Myo5c mediate transport of several different cargoes. All MyoV paralogs bind to cargo complexes mainly by their C-terminal globular domains. In absence of cargo, the globular domain of Myo5a inhibits its motor domain. Here, we report low-resolution SAXS models for the globular domains from human Myo5a, Myo5b, and Myo5c, which suggest very similar overall shapes of all three paralogs. We determined the crystal structures of globular domains from Myo5a and Myo5b, and provide a homology model for human Myo5c. When we docked the Myo5a crystal structure into a previously published electron microscopy density of the autoinhibited full-length Myo5a, only one domain orientation resulted in a good fit. This structural arrangement suggests the participation of additional region of the globular domain in autoinhibition. Quantification of the interaction of the Myo5a globular domain with its motor complex revealed a tight binding with dissociation half-life in the order of minutes, suggesting a rather slow transition between the active and inactive states.

Structural insights into the globular tails of the human type v myosins myo5a, myo5b, and myo5c.,Velvarska H, Niessing D PLoS One. 2013 Dec 10;8(12):e82065. doi: 10.1371/journal.pone.0082065. PMID:24339992^[4]

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

References

↑ 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
↑ 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
↑ 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
↑ Velvarska H, Niessing D. Structural insights into the globular tails of the human type v myosins myo5a, myo5b, and myo5c. PLoS One. 2013 Dec 10;8(12):e82065. doi: 10.1371/journal.pone.0082065. PMID:24339992 doi:http://dx.doi.org/10.1371/journal.pone.0082065

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/4lnz"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human Myosin 5b globular domain==
 <StructureSection load='4lnz' size='340' side='right' caption='[[4lnz]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lli|4lli]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO5B, KIAA1119 ([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=4lnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lnz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lnz RCSB], [http://www.ebi.ac.uk/pdbsum/4lnz 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=4lnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lnz OCA], [http://pdbe.org/4lnz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lnz RCSB], [http://www.ebi.ac.uk/pdbsum/4lnz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lnz ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4lnz" style="background-color:#fffaf0;"></div>
 ==See Also==

4lnz

From Proteopedia

Revision as of 17:39, 5 August 2016

Crystal structure of human Myosin 5b globular domain

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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