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Protein dimer

From Wikipedia, the free encyclopedia
(Redirected fromHeterodimers)
Macromolecular complex formed by two, usually non-covalently bound, macromolecules
Ribbon diagram of a dimer ofEscherichia coligalactose-1-phosphate uridylyltransferase (GALT) in complex withUDP-galactose. Potassium, zinc, and iron ions are visible as purple, gray, and bronze-colored spheres respectively.

Inbiochemistry, aprotein dimer is amacromolecular complex ormultimer formed by twoprotein monomers, or single proteins, which are usuallynon-covalently bound. Many macromolecules, such as proteins ornucleic acids, form dimers. The worddimer has roots meaning "two parts",di- +-mer. A protein dimer is a type ofprotein quaternary structure.

A proteinhomodimer is formed by two identicalproteins while a proteinheterodimer is formed by two different proteins.

Most protein dimers in biochemistry are not connected bycovalent bonds. An example of a non-covalent heterodimer is the enzymereverse transcriptase, which is composed of two differentamino acid chains.[1] An exception is dimers that are linked bydisulfide bridges such as the homodimeric proteinNEMO.[2]

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

TheG protein-coupledcannabinoid receptors have the ability to form both homo- and heterodimers with several types of receptors such asmu-opioid,dopamine andadenosine A2 receptors.[4]

Examples

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Alkaline phosphatase

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E. colialkaline phosphatase, a dimer enzyme, exhibitsintragenic complementation.[5] That is, when particularmutant versions of alkaline phosphatase were combined, the heterodimeric enzymes formed as a result exhibited a higher level of activity than would be expected based on the relative activities of the parental enzymes. These findings indicated that the dimer structure of theE. coli alkaline phosphatase allows cooperative interactions between the constituent mutant monomers that can generate a more functional form of theholoenzyme. The dimer has two active sites, each containing two zinc ions and a magnesium ion.[6]

See also

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References

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  1. ^Sluis-Cremer N, Hamamouch N, San Félix A, Velazquez S, Balzarini J, Camarasa MJ (August 2006). "Structure-activity relationships of [2',5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]- 3'-spiro-5' '-(4' '-amino-1' ',2' '-oxathiole-2' ',2' '-dioxide)thymine derivatives as inhibitors of HIV-1 reverse transcriptase dimerization".J. Med. Chem.49 (16):4834–41.doi:10.1021/jm0604575.PMID 16884295.
  2. ^Herscovitch M, Comb W, Ennis T, Coleman K, Yong S, Armstead B, Kalaitzidis D, Chandani S, Gilmore TD (February 2008)."Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347".Biochemical and Biophysical Research Communications.367 (1):103–8.doi:10.1016/j.bbrc.2007.12.123.PMC 2277332.PMID 18164680.
  3. ^Amoutzias, Grigoris D.; Robertson, David L.; Van de Peer, Yves; Oliver, Stephen G. (2008-05-01). "Choose your partners: dimerization in eukaryotic transcription factors".Trends in Biochemical Sciences.33 (5):220–229.doi:10.1016/j.tibs.2008.02.002.ISSN 0968-0004.PMID 18406148.
  4. ^Filipiuc, Leontina Elena; Ababei, Daniela Carmen; Alexa-Stratulat, Teodora; Pricope, Cosmin Vasilica; Bild, Veronica; Stefanescu, Raluca; Stanciu, Gabriela Dumitrita; Tamba, Bogdan-Ionel (2021-11-01)."Major Phytocannabinoids and Their Related Compounds: Should We Only Search for Drugs That Act on Cannabinoid Receptors?".Pharmaceutics.13 (11): 1823.doi:10.3390/pharmaceutics13111823.ISSN 1999-4923.PMC 8625816.PMID 34834237.
  5. ^Hehir, Michael J.; Murphy, Jennifer E.; Kantrowitz, Evan R. (2000). "Characterization of Heterodimeric Alkaline Phosphatases from Escherichia coli: An Investigation of Intragenic Complementation".Journal of Molecular Biology.304 (4):645–656.doi:10.1006/jmbi.2000.4230.PMID 11099386.
  6. ^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 (BBA) - Proteins and Proteomics, vol. 1864, no. 7, 2016, pp. 755–765,https://doi.org/10.1016/j.bbapap.2016.03.016.
  • Conn. (2013).G protein coupled receptors modeling, activation, interactions and virtual screening (1st ed.). Academic Press.
  • Matthews, Jacqueline M.Protein Dimerization and Oligomerization in Biology. Springer New York, 2012.
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