Protein dimer
In
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
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
- Transcription factors
- Leucine zipper motif proteins
- 14-3-3 proteins
- Variable surface glycoproteinsof the Trypanosoma parasite
- Tubulin
- Some clotting factors
- Some receptors
- Nuclear receptors
- G protein βγ-subunit dimer
- Toll-like receptor
- Receptor tyrosine kinases
- Some enzymes
- Type II restriction enzymes
- Triosephosphateisomerase(TIM)
- Alcohol dehydrogenase
Alkaline phosphatase
E. coli
See also
- Dimer (chemistry)
- Protein trimer
- Oligomer
- ProtCID
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.