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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/20 15:40:30」(JST)

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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 biochemistry, a dimer is a macromolecular complex formed by two, usually non-covalently bound, macromolecules such as proteins or nucleic acids. It is a quaternary structure of a protein.

A homodimer is formed by two identical molecules (a process called homodimerisation). A heterodimer is formed by two different macromolecules (called heterodimerisation).

Most 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).

Examples

Antibodies
Receptor tyrosine kinases
Transcription factors
- Leucine zipper motif proteins
- Nuclear receptors
14-3-3 proteins
G protein-coupled receptors
G protein βγ-subunit dimer
Kinesin
Triosephosphateisomerase (TIM)
Alcohol dehydrogenase
Factor XI
Factor XIII
Toll-like receptor
Fibrinogen
Variable surface glycoproteins of the Trypanosoma parasite

References

^ 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. PMC 2277332. PMID 18164680.

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English Journal

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Allonso D, Pereira IB, Alves AM, Kurtenbach E, Mohana-Borges R.
Protein expression and purification. 2019 Oct;162()9-17.
The dengue virus (DENV) non structural protein 1 (NS1) is a 46-55 kDa protein that exists as homodimer inside cells and as hexamer in the extracellular milieu. Several lines of evidence have demonstrated that the biochemical and structural properties of recombinant NS1 (rNS1) vary depending on the
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Structural and DNA-binding studies of the PadR-like transcriptional regulator BC1756 from Bacillus cereus.

Kim TH, Park SC, Lee KC, Song WS, Yoon SI.
Biochemical and biophysical research communications. 2019 Aug;515(4)607-613.
Transcription factors that belong to the PadR family play an essential role in the transcriptional regulation of diverse biological processes by recognizing their cognate palindromic DNA sequences. Bacillus cereus harbors a gene that encodes a PadR-like protein (bcPLP; BC1756). bcPLP has not been st
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Death domain of p75 neurotrophin receptor: a structural perspective on an intracellular signalling hub.

Yuan W, Ibáñez CF, Lin Z.
Biological reviews of the Cambridge Philosophical Society. 2019 Aug;94(4)1282-1293.
The death domain (DD) is a globular protein motif with a signature feature of an all-helical Greek-key motif. It is a primary mediator of a variety of biological activities, including apoptosis, cell survival and cytoskeletal changes, which are related to many neurodegenerative diseases, neurotrauma
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Japanese Journal

Characterization of Proanthocyanidin Oligomers of Ephedra sinica

Molecules 22(8), 1308, 2017-08-06
NAID 120006346208

A Quantitative Study of Internal and External Interactions of Homodimeric Glucocorticoid Receptor Using Fluorescence Cross-Correlation Spectroscopy in a Live Cell