4r1e: Difference between revisions
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<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=4r1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r1e RCSB], [http://www.ebi.ac.uk/pdbsum/4r1e 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=4r1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r1e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r1e RCSB], [http://www.ebi.ac.uk/pdbsum/4r1e PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/MYOA_PLAF7 MYOA_PLAF7]] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments (By similarity). | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |