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This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
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Contents |
Heavy Meromyosin
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Organism of Origin
This protein originated in tarantulas, Red Junglefowls and humans.
Protein Structure
Heavy meromyosin (HMM) is a subunit of myosin. There are two fragments that make up HMM: S-1 and S-2. S-1 projects out on an angle whereas S-2 is comprised of globular heads that can bind to actin. Together, these are called a myosin cross bridge. There are four distinct macromolecules that comprise HMM, including (196 amino acids: magenta), (150 amino acids: blue), (971 amino acids: gold), and (973 amino acids: purple).
Function
Heavy meromyosin is a part of the actin-myosin system. Heavy meromyosin (and light meromyosin) are subunits of myosin. HMM is the globular head portion of myosin which determines the rate of muscle contraction in an organism. Actin binding capacity and ATPase activity are dependent on HMM.
Significance
Heavy meromyosin is important for muscle contractions in a multitude of organisms. It plays an important role in microtubule-based movement as a part of the myosin complex. The ability for myosin to bind to actin and use ATP to create mechanical energy is dependent on heavy meromyosin. Without this protein, muscle contraction and mobility would be limited.
References
https://www.ncbi.nlm.nih.gov/pubmed/27591903
https://www.ncbi.nlm.nih.gov/books/NBK9961/
https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/heavy-meromyosin