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2kia

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Solution structure of Myosin VI C-terminal cargo-binding domain

Structural highlights

2kia is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

MYO6_MOUSE Note=Defects in Myo6 are the cause of Snell's waltzer, a condition characterized by circling, head-tossing, deafness and hyperactivity.

Function

MYO6_MOUSE Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.

Myosin VI undergoes cargo-mediated dimerization.,Yu C, Feng W, Wei Z, Miyanoiri Y, Wen W, Zhao Y, Zhang M Cell. 2009 Aug 7;138(3):537-48. PMID:19665975^[1]

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

References

↑ Yu C, Feng W, Wei Z, Miyanoiri Y, Wen W, Zhao Y, Zhang M. Myosin VI undergoes cargo-mediated dimerization. Cell. 2009 Aug 7;138(3):537-48. PMID:19665975 doi:10.1016/j.cell.2009.05.030

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2kia"

@@ Line 1: / Line 1: @@
-[[Image:2kia.png|left|200px]]
-{{STRUCTURE_2kia|  PDB=2kia  |  SCENE=  }}
+==Solution structure of Myosin VI C-terminal cargo-binding domain==
+<StructureSection load='2kia' size='340' side='right'caption='[[2kia]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2kia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KIA FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2kia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kia OCA], [https://pdbe.org/2kia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kia RCSB], [https://www.ebi.ac.uk/pdbsum/2kia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kia ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/MYO6_MOUSE MYO6_MOUSE] Note=Defects in Myo6 are the cause of Snell's waltzer, a condition characterized by circling, head-tossing, deafness and hyperactivity.
+== Function ==
+[https://www.uniprot.org/uniprot/MYO6_MOUSE MYO6_MOUSE] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ki/2kia_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kia ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Myosin VI is the only known molecular motor that moves toward the minus ends of actin filaments; thus, it plays unique roles in diverse cellular processes. The processive walking of myosin VI on actin filaments requires dimerization of the motor, but the protein can also function as a nonprocessive monomer. The molecular mechanism governing the monomer-dimer conversion is not clear. We report the high-resolution NMR structure of the cargo-free myosin VI cargo-binding domain (CBD) and show that it is a stable monomer in solution. The myosin VI CBD binds to a fragment of the clathrin-coated vesicle adaptor Dab2 with a high affinity, and the X-ray structure of the myosin VI CBD in complex with Dab2 reveals that the motor undergoes a cargo-binding-mediated dimerization. The cargo-binding-induced dimerization may represent a general paradigm for the regulation of processivity for myosin VI as well as other myosins, including myosin VII and myosin X.
-===Solution structure of Myosin VI C-terminal cargo-binding domain===
+Myosin VI undergoes cargo-mediated dimerization.,Yu C, Feng W, Wei Z, Miyanoiri Y, Wen W, Zhao Y, Zhang M Cell. 2009 Aug 7;138(3):537-48. PMID:19665975<ref>PMID:19665975</ref>
-{{ABSTRACT_PUBMED_19665975}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 2kia" style="background-color:#fffaf0;"></div>
-[[2kia]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KIA OCA].
 ==See Also==
-*[[Myosin|Myosin]]
+*[[Myosin 3D Structures|Myosin 3D Structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:019665975</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Feng, W.]]
+[[Category: Feng W]]
-[[Category: Miyanoiri, Y.]]
+[[Category: Miyanoiri Y]]
-[[Category: Wei, Z.]]
+[[Category: Wei Z]]
-[[Category: Yu, C.]]
+[[Category: Yu C]]
-[[Category: Zhang, M.]]
+[[Category: Zhang M]]
-[[Category: Actin-binding]]
-[[Category: Atp-binding]]
-[[Category: Calmodulin-binding]]
-[[Category: Cargo-binding domain]]
-[[Category: Cell projection]]
-[[Category: Coated pit]]
-[[Category: Cytoplasmic vesicle]]
-[[Category: Deafness]]
-[[Category: Disease mutation]]
-[[Category: Endocytosis]]
-[[Category: Golgi apparatus]]
-[[Category: Hearing]]
-[[Category: Membrane]]
-[[Category: Molecular motor]]
-[[Category: Motor protein]]
-[[Category: Myosin]]
-[[Category: Myosin vi]]
-[[Category: Nucleotide-binding]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Protein transport]]
-[[Category: Transport]]

2kia

From Proteopedia

Current revision

Solution structure of Myosin VI C-terminal cargo-binding domain

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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