5wfn | pdb_00005wfn
Revised model of leiomodin 2-mediated actin regulation (alternate refinement of PDB 4RWT)
Structural highlights
Function[ACT1_DROME] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. [LMOD2_HUMAN] Increases the rate of actin polymerization (PubMed:25250574).[1] Publication Abstract from PubMedLeiomodin (Lmod) is a class of potent tandem-G-actin-binding nucleators in muscle cells. Lmod mutations, deletion, or instability are linked to lethal nemaline myopathy. However, the lack of high-resolution structures of Lmod nucleators in action severely hampered our understanding of their essential cellular functions. Here we report the crystal structure of the actin-Lmod2162-495 nucleus. The structure contains two actin subunits connected by one Lmod2162-495 molecule in a non-filament-like conformation. Complementary functional studies suggest that the binding of Lmod2 stimulates ATP hydrolysis and accelerates actin nucleation and polymerization. The high level of conservation among Lmod proteins in sequence and functions suggests that the mechanistic insights of human Lmod2 uncovered here may aid in a molecular understanding of other Lmod proteins. Furthermore, our structural and mechanistic studies unraveled a previously unrecognized level of regulation in mammalian signal transduction mediated by certain tandem-G-actin-binding nucleators. Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.,Chen X, Ni F, Kondrashkina E, Ma J, Wang Q Proc Natl Acad Sci U S A. 2015 Oct 13;112(41):12687-92. doi:, 10.1073/pnas.1512464112. Epub 2015 Sep 28. PMID:26417072[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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