Protein dimer

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Heterodimer
)
Cartoon diagram of a dimer of Escherichia coli galactose-1-phosphate uridylyltransferase (GALT) in complex with UDP-galactose (stick models). Potassium, zinc, and iron ions are visible as purple, gray, and bronze-colored spheres respectively.

In

multimer formed by two protein monomers, or single proteins, which are usually non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers. The word dimer has roots meaning "two parts", di- + -mer. A protein dimer is a type of protein quaternary structure
.

A protein homodimer is formed by two identical proteins while a protein heterodimer is formed by two different proteins.

Most protein dimers in biochemistry are not connected by

disulfide bridges such as the homodimeric protein NEMO.[2]

Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity.[3]

The G protein-coupled cannabinoid receptors have the ability to form both homo- and heterodimers with several types of receptors such as mu-opioid, dopamine and adenosine A2 receptors.[4]

Examples

Alkaline phosphatase

E. coli

holoenzyme
. The dimer has two active sites, each containing two zinc ions and a magnesium ion.[8]

See also

References

6. Conn. (2013). G protein coupled receptors modeling, activation, interactions and virtual screening (1st ed.). Academic Press.

7. Matthews, Jacqueline M. Protein Dimerization and Oligomerization in Biology. Springer New York, 2012.

8. Hjorleifsson, Jens Gu[eth]Mundur, and Bjarni Asgeirsson. “Cold-Active Alkaline Phosphatase Is Irreversibly Transformed into an Inactive Dimer by Low Urea Concentrations.” Biochimica et Biophysica Acta. Proteins and Proteomics, vol. 1864, no. 7, 2016, pp. 755–765, https://doi.org/10.1016/j.bbapap.2016.03.016.