4lli: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lli]] 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=4LLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LLI FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lli]] 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=4LLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LLI FirstGlance]. <br>
</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=4lli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lli OCA], [https://pdbe.org/4lli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lli RCSB], [https://www.ebi.ac.uk/pdbsum/4lli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lli ProSAT]</span></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]] 2.2&#8491;</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=4lli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lli OCA], [https://pdbe.org/4lli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lli RCSB], [https://www.ebi.ac.uk/pdbsum/4lli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lli ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/MYO5A_HUMAN 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.<ref>PMID:10448864</ref>  
[https://www.uniprot.org/uniprot/MYO5A_HUMAN 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.<ref>PMID:10448864</ref>  
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24339992</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lli" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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