Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural basis of nonmuscle myosin-2 autoinhibition mechanisms.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	Jun 26, 2026
Authors	Sarah M Heissler / Giovanna Grandinetti / James R Sellers / Krishna Chinthalapudi /
PubMed Abstract	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 ...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.
External links	Nat Commun / PubMed:42323327
Methods	EM (single particle)
Resolution	4.1 - 10.0 Å
Structure data	73793 EMDB Unreleased entry 9z3w EMDB-73793, PDB-9z3w: Cryo-EM structure of human nonmuscle myosin-2B, Class 1 Method: EM (single particle) / Resolution: 5.34 Å 73796 EMDB Unreleased entry 9z3z EMDB-73796, PDB-9z3z: Cryo-EM structure of human nonmuscle myosin-2B, Class 2 Method: EM (single particle) / Resolution: 5.24 Å 73797 EMDB Unreleased entry 9z40 EMDB-73797, PDB-9z40: Cryo-EM structure of full-length human NM2B Method: EM (single particle) / Resolution: 10.0 Å EMDB Unreleased entry EMDB-73798: Cryo-EM map of human NM2B 10S state Method: EM (single particle) / Resolution: 9.83 Å 73811 EMDB Unreleased entry 9z4q EMDB-73811, PDB-9z4q: Cryo-EM structure of human nonmuscle myosin-2B, Class 3 Method: EM (single particle) / Resolution: 4.1 Å EMDB Unreleased entry EMDB-73815: Cryo-EM map of tail region of NM2B 10S state - class 1 Method: EM (single particle) / Resolution: 6.64 Å EMDB Unreleased entry EMDB-73818: Cryo-EM map of tail region of NM2B 10S state - class 2 Method: EM (single particle) / Resolution: 7.6 Å EMDB Unreleased entry EMDB-77751: NM2B full-length Consensus map Method: EM (single particle) / Resolution: 10.0 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION ChemComp-MG*: Unknown entry
Source	homo sapiens (human)
Keywords	MOTOR PROTEIN / myosin / ATPase / ATPase enzyme