5hmo: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5hmo is ~~ON HOLD until Paper Publication~~

==myosin X motor activity==

~~Authors~~: ~~Ropars~~, V., ~~Blanc~~, F., ~~Samazan~~, F., ~~Houdusse~~, A.

== Structural highlights ==

<table><tr><td colspan='2'>[[5hmo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HMO FirstGlance]. <br>

~~Description~~: ~~myosin X motor activity~~

</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=5hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmo OCA], [http://pdbe.org/5hmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hmo RCSB], [http://www.ebi.ac.uk/pdbsum/5hmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hmo ProSAT]</span></td></tr>

[[Category: ~~Unreleased Structures~~]]

</table>

== Function ==

[[http://www.uniprot.org/uniprot/MYO10_BOVIN MYO10_BOVIN]] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.<ref>PMID:11457842</ref> <ref>PMID:15156152</ref> <ref>PMID:15705568</ref> <ref>PMID:16894163</ref> <ref>PMID:20081229</ref> <ref>PMID:20364131</ref> <ref>PMID:20392702</ref> <ref>PMID:20930142</ref> <ref>PMID:21666676</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Blanc, F]]

[[Category: Houdusse, A]]

[[Category: Ropars, V]]

[[Category: Samazan, F]]

[[Category: ~~Blanc, F~~]]

[[Category: Motor protein]]

[[Category: ~~Houdusse, A~~]]

[[Category: Myosin]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5hmo is ON HOLD  until Paper Publication
+==myosin X motor activity==
+<StructureSection load='5hmo' size='340' side='right' caption='[[5hmo]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
-Authors: Ropars, V., Blanc, F., Samazan, F., Houdusse, A.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5hmo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HMO FirstGlance]. <br>
-Description: myosin X motor activity
+</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=5hmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hmo OCA], [http://pdbe.org/5hmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hmo RCSB], [http://www.ebi.ac.uk/pdbsum/5hmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hmo ProSAT]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/MYO10_BOVIN MYO10_BOVIN]] In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation (By similarity). Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as plus end-directed motor. The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate, which are then moved relative to actin filaments. Stimulates the formation and elongation of filopodia. Regulates cell shape, cell spreading and cell adhesion. Plays a role in formation of the podosome belt in osteoclasts.<ref>PMID:11457842</ref> <ref>PMID:15156152</ref> <ref>PMID:15705568</ref> <ref>PMID:16894163</ref> <ref>PMID:20081229</ref> <ref>PMID:20364131</ref> <ref>PMID:20392702</ref> <ref>PMID:20930142</ref> <ref>PMID:21666676</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Blanc, F]]
+[[Category: Houdusse, A]]
 [[Category: Ropars, V]]
 [[Category: Samazan, F]]
-[[Category: Blanc, F]]
+[[Category: Motor protein]]
-[[Category: Houdusse, A]]
+[[Category: Myosin]]