The structure of the F-actin filament and the actin molecule
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Differential N-terminal processing of beta and gamma actin
2022, iScienceCitation Excerpt :This suggests that processed beta actin is otherwise functional and can incorporate into filaments and undergo disassembly regardless of its N-terminus. An attractive possibility is that processed actin subunits within filaments and/or the monomer pool can affect interactions with actin-binding proteins that are attracted or repelled by the negatively charged actin N-terminal tails exposed on the actin subunit surface (Holmes et al., 1982; Kabsch et al., 1985; Bremer and Aebi, 1992; Chik et al., 1996; Rebowski et al., 2020). Locally applied, such attraction or repulsion can potentially have a profound effect on actin function.
Dynamical mechanism of stepping of the molecular motor myosin V along actin filament and simulation in an actual system
2019, Physica A: Statistical Mechanics and its ApplicationsCitation Excerpt :Also, I verify the applicability of the dynamical mechanism with a simulation experiment preserving most of the known characteristics of myosin–actin complex [2]. The structure of the actin filament comprises two twisted strands of the actin monomers [27–29]. The actin monomer can be considered as a brick with a square face that is 5.5 nm in width and 3.5 nm in height [24].
Unconventional actin configurations step into the limelight
2013, Advances in Protein Chemistry and Structural BiologyCitation Excerpt :These interactions, together with its inherent plasticity, render actin one of the most versatile proteins in the eukaryotic cell, both with respect to structure and function. Due to its propensity to form noncrystalline filamentous aggregates or paracrystalline arrays under the conditions normally used for crystallization (Bremer & Aebi, 1992), monomeric actin has for long resisted crystallization attempts. Different strategies employed to prevent actin from polymerizing, including point mutations, covalent modification, or association with other proteins or ligands, finally allowed its structure to be determined at atomic resolution (Fig. 5.1; Kabsch et al., 1990).
Two deafness-causing (DFNA20/26) actin mutations affect Arp2/3-dependent actin regulation
2012, Journal of Biological ChemistryThree-dimensional cryo-electron microscopy on intermediate filaments
2010, Methods in Cell BiologyStructural analysis of vimentin and keratin intermediate filaments by cryo-electron tomography
2007, Experimental Cell Research