3au4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:02, 13 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='3au4' size='340' side='right'caption='[[3au4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3au4' size='340' side='right'caption='[[3au4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3au4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AU4 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3au4]] is a 2 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=3AU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AU4 FirstGlance]. <br>
-
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3au5|3au5]]</div></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]] 1.9&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO10, KIAA0799 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), DCC, IGDCC1 ([https://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=3au4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3au4 OCA], [https://pdbe.org/3au4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3au4 RCSB], [https://www.ebi.ac.uk/pdbsum/3au4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3au4 ProSAT]</span></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=3au4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3au4 OCA], [https://pdbe.org/3au4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3au4 RCSB], [https://www.ebi.ac.uk/pdbsum/3au4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3au4 ProSAT]</span></td></tr>
</table>
</table>
-
== Disease ==
 
-
[[https://www.uniprot.org/uniprot/DCC_HUMAN DCC_HUMAN]] Defects in DCC are the cause of mirror movements type 1 (MRMV1) [MIM:[https://omim.org/entry/157600 157600]]. A disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities.<ref>PMID:20431009</ref>
 
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/MYO10_HUMAN MYO10_HUMAN]] 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 or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. Plays a role in formation of the podosome belt in osteoclasts (By similarity).<ref>PMID:16894163</ref> [[https://www.uniprot.org/uniprot/DCC_HUMAN DCC_HUMAN]] Receptor for netrin required for axon guidance. Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Its association with UNC5 proteins may trigger signaling for axon repulsion. It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand. Implicated as a tumor suppressor gene.<ref>PMID:8861902</ref> <ref>PMID:8187090</ref>
+
[https://www.uniprot.org/uniprot/MYO10_HUMAN MYO10_HUMAN] 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 or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. May play a role in neurite outgrowth and axon guidance. Plays a role in formation of the podosome belt in osteoclasts (By similarity).<ref>PMID:16894163</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Myosin-X is an important unconventional myosin that is critical for cargo transportation to filopodia tips and is also utilized in spindle assembly by interacting with microtubules. We present a series of structural and biochemical studies of the myosin-X tail domain cassette, consisting of myosin tail homology 4 (MyTH4) and FERM domains in complex with its specific cargo, a netrin receptor DCC (deleted in colorectal cancer). The MyTH4 domain is folded into a helical VHS-like structure and is associated with the FERM domain. We found an unexpected binding mode of the DCC peptide to the subdomain C groove of the FERM domain, which is distinct from previously reported beta-beta associations found in radixin-adhesion molecule complexes. We also revealed direct interactions between the MyTH4-FERM cassette and tubulin C-terminal acidic tails, and identified a positively charged patch of the MyTH4 domain, which is involved in tubulin binding. We demonstrated that both DCC and integrin bindings interfere with microtubule binding and that DCC binding interferes with integrin binding. Our results provide the molecular basis by which myosin-X facilitates alternative dual binding to cargos and microtubules.
+
-
 
+
-
Structural basis of cargo recognition by the myosin-X MyTH4-FERM domain.,Hirano Y, Hatano T, Takahashi A, Toriyama M, Inagaki N, Hakoshima T EMBO J. 2011 Jun 3;30(13):2734-47. doi: 10.1038/emboj.2011.177. PMID:21642953<ref>PMID:21642953</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3au4" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 29: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Hakoshima, T]]
+
[[Category: Hakoshima T]]
-
[[Category: Hatano, T]]
+
[[Category: Hatano T]]
-
[[Category: Hirano, Y]]
+
[[Category: Hirano Y]]
-
[[Category: Motor protein cargo transportation]]
+
-
[[Category: Motor protein-apoptosis complex]]
+
-
[[Category: Protein-protein complex]]
+

Current revision

Structure of the human myosin-X MyTH4-FERM cassette bound to its specific cargo, DCC

PDB ID 3au4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3au4"
Personal tools