Binding domain explained

In molecular biology, binding domain is a protein domain which binds to a specific atom or molecule, such as calcium or DNA. A protein domain is a part of a protein sequence and a tertiary structure that can change or evolve, function, and live by itself independent of the rest of the protein chain.^[1] Upon binding, proteins may undergo a conformational change. Binding domains are essential for the function of many proteins. They are essential because they help splice, assemble, and translate proteins.^[2]

Examples of binding domains include the Zinc finger, which binds to DNA, and EF hand, which binds to calcium.

See also

• DNA-binding domain
• Receptor (biochemistry)

Notes and References

1. Phillips, DC. (1966). "The three-dimensional structure of an enzyme molecule". Scientific American. 215 (5): 78–90. . .
2. Yong, J., T. J. Golembe, D. J. Battle, L. Pellizzoni, and G. Dreyfuss. "SnRNAs Contain Specific SMN-binding Domains That Are Essential for SnRNP Assembly". Molecular and Cellular Biology. U.S. National Library of Medicine, April 2004. Retrieved April 2017.