Jump to content

User:ListeningLearner29/Myosin

From Wikipedia, the free encyclopedia
Self-inhibition of Myosin II [1][2][4]. The movie begins with Myosin II in the 10S conformation with a folded tail domain, the blocked head and free head [2][3]. The movie schematically depicts tail unfolding and the resulting active 6S confirmation [2][3] followed by tail folding back to the 10S conformation. The illustration is conceptual: transitory states and diffusive motions associated with folding/unfolding are not shown [4].

Article Draft

[edit]

Lead

[edit]

Article body

[edit]

Myosin II[edit]

[edit]

Myosin II (also known as conventional myosin) is the myosin type responsible for producing muscle contraction in muscle cells in most animal cell types. It is also found in non-muscle cells in contractile bundles called stress fibers.

  • Myosin II contains two heavy chains, each about 2000 amino acids in length, which constitute the head and tail domains. Each of these heavy chains contains the N-terminal head domain, while the C-terminal tails take on a coiled-coil morphology, holding the two heavy chains together (imagine two snakes wrapped around each other, as in a caduceus). Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. In smooth muscle, a single gene (MYH11)) codes for the heavy chains myosin II, but splice variants of this gene result in four distinct isoforms.
  • It also contains 4 myosin light chains (MLC), resulting in 2 per head, weighing 20 (MLC20) and 17 (MLC17) kDa. These bind the heavy chains in the "neck" region between the head and tail.
    • The MLC20 is also known as the regulatory light chain and actively participates in muscle contraction.
    • The MLC17 is also known as the essential light chain. Its exact function is unclear, but is believed to contribute to the structural stability of the myosin head along with MLC20. Two variants of MLC17 (MLC17a/b) exist as a result of alternative splicing at the MLC17 gene.

In muscle cells, the long coiled-coil tails of the individual myosin molecules can auto-inhibit active function in the 10S conformation or upon phosphorylation, change to the 6S conformation and join, forming the thick filaments of the sarcomere. [3][4] The force-producing head domains stick out from the side of the thick filament, ready to walk along the adjacent actin-based thin filaments in response to the proper chemical signals and may be in either auto-inhibited or active conformation. The balance/transition between active and inactive states is subject to extensive chemical regulation.

Further information: Muscle contraction

Further information: Meromyosin

References

[edit]