4pl8

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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=4pl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4pl8 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=4pl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pl8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4pl8 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 09:20, 25 December 2014

Structure of rabbit skeletal muscle actin in complex with a hybrid peptide comprising thymosin beta4 and the lysine-rich region of Cordon-Bleu

4pl8, resolution 2.00Å

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