9z3z

Cryo-EM structure of human nonmuscle myosin-2B, Class 2

spinqualitylabelsall models 9z3z, resolution 5.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9z3z is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 5.24Å Ligands: ADP, MG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MYH10_HUMAN Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. During cell spreading, plays an important role in cytoskeleton reorganization, focal contacts formation (in the central part but not the margins of spreading cells), and lamellipodial extension; this function is mechanically antagonized by MYH9. Publication Abstract from PubMed Nonmuscle myosin-2 (NM2) is a fundamental actin-based mechanochemical ATPase that regulates cellular architecture, migration, adhesion, and force generation across diverse biological contexts. NM2 function is tightly regulated by a structural transition between an autoinhibited monomeric (10S) conformation in which ATPase activity, actin binding, and filament assembly are coordinately suppressed and an enzymatically active, filamentous conformation. The autoinhibited conformation is critical for the spatial and temporal control of contractility in nonmuscle cells, yet structural insights into the 10S conformation remain largely elusive. Here, we report a ~53-nm elongated full-length structure of NM2B in the 10S conformation and four distinct cryo-EM structures representing the conformational landscape within the human NM2B 10S state. These structures reveal a tri-segmented tail fold that sequesters interfaces essential for actin binding and filament assembly. The asymmetric arrangement of myosin heavy and light chains provides a mechanistic foundation for understanding how regulatory post-translational modifications and disease-associated mutations shift NM2 conformational equilibria and may enable the development of structure-based interventions for cytoskeletal diseases including hearing loss, neurodegeneration, and cancer. Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.,Heissler SM, Grandinetti G, Sellers JR, Chinthalapudi K Nat Commun. 2026 Jun 20. doi: 10.1038/s41467-026-74674-w. PMID:42323327 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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