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.
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 covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, which is composed of two different amino acid chains.[1] An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO.[2]
Some proteins contain specialized domains to ensure dimerization (dimerization domains) and specificity.[3]
E. colialkaline phosphatase, a dimer enzyme, exhibits intragenic complementation.[5] That is, when particular mutant 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 the E. coli alkaline phosphatase allows cooperative interactions between the constituent mutant monomers that can generate a more functional form of the holoenzyme. The dimer has two active sites, each containing two zinc ions and a magnesium ion.[8]
^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.
^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. PMC2277332. PMID 18164680.
^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.
^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. PMC8625816. PMID 34834237.
^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. 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.
protein, dimer, biochemistry, protein, dimer, macromolecular, complex, multimer, formed, protein, monomers, single, proteins, which, usually, covalently, bound, many, macromolecules, such, proteins, nucleic, acids, form, dimers, word, dimer, roots, meaning, pa. In biochemistry a protein dimer is a macromolecular complex or 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 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 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 covalent bonds An example of a non covalent heterodimer is the enzyme reverse transcriptase which is composed of two different amino acid chains 1 An exception is dimers that are linked 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 Contents 1 Examples 2 Alkaline phosphatase 3 See also 4 ReferencesExamples editTranscription factors Leucine zipper motif proteins 14 3 3 proteins Variable surface glycoproteins of the Trypanosoma parasite Tubulin Some clotting factors Factor XI Factor XIII Fibrinogen Some receptors Nuclear receptors G protein bg subunit dimer Toll like receptor Receptor tyrosine kinases Some enzymes Type II restriction enzymes Triosephosphateisomerase TIM Alcohol dehydrogenaseAlkaline phosphatase editE coli alkaline phosphatase a dimer enzyme exhibits intragenic complementation 5 That is when particular mutant 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 the E coli alkaline phosphatase allows cooperative interactions between the constituent mutant monomers that can generate a more functional form of the holoenzyme The dimer has two active sites each containing two zinc ions and a magnesium ion 8 See also editDimer chemistry Protein trimer Oligomer ProtCIDReferences edit Sluis Cremer N Hamamouch N San Felix 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 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 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 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 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 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 Portal nbsp Biology Retrieved from https en wikipedia org w index php title Protein dimer amp oldid 1188517395, wikipedia, wiki, book, books, library,
