3m6g

Crystal structure of actin in complex with lobophorolide

spinqualitylabelsall models 3m6g, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3m6g is a 2 chain structure with sequence from Lobophora variegata and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, CA, LO3, MG Related: 1yxq, 2vyp, 2asm, 2aso, 2asp, 1qz5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMed Actin filament-disrupting marine macrolides are promising templates from which to design therapeutics against cancer and other diseases that co-opt the actin cytoskeleton. Typically, these macrolides form either a 1:1 or 2:1 actin-macrolide complex where their aliphatic side chain, or "tail," has been reported to convey the major determinant of cytotoxicity. We now report the structure of the marine macrolide lobophorolide bound to actin with a unique 2:2 stoichiometry in which two lobophorolide molecules cooperate to form a dimerization interface that is composed entirely of the macrolide "ring" region, and each molecule of lobophorolide interacts with both actin subunits via their ring and tail regions to tether the subunits together. This binding mode imposes multiple barriers against microfilament stability and holds important implications for development of actin-targeting drugs and the evolution of macrolide biosynthetic enzymes. Two molecules of lobophorolide cooperate to stabilize an actin dimer using both their "ring" and "tail" region.,Blain JC, Mok YF, Kubanek J, Allingham JS Chem Biol. 2010 Aug 27;17(8):802-7. PMID:20797609 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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