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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/08/07 11:43:28」(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.

UpToDate Contents

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English Journal

Intrinsic and extrinsic regulation of cardiac lipoprotein lipase following diabetes.

Wang Y1, Rodrigues B2.
Biochimica et biophysica acta.Biochim Biophys Acta.2015 Feb;1851(2):163-171. doi: 10.1016/j.bbalip.2014.11.007. Epub 2014 Nov 18.
Cardiac lipoprotein lipase (LPL) is a pivotal enzyme controlling heart metabolism by providing the majority of fatty acids required by this organ. From activation in cardiomyocytes to secretion to the vascular lumen, cardiac LPL is regulated by multiple pathways, which are altered during diabetes. H
PMID 25463481

Role of the focal adhesion protein TRIM15 in colon cancer development.

Lee OH1, Lee J2, Lee KH2, Woo YM1, Kang JH3, Yoon HG4, Bae SK5, Songyang Z6, Oh SH3, Choi Y7.
Biochimica et biophysica acta.Biochim Biophys Acta.2015 Feb;1853(2):409-21. doi: 10.1016/j.bbamcr.2014.11.007. Epub 2014 Nov 15.
The tripartite motif containing (TRIM) proteins are a large family of proteins that have been implicated in many biological processes including cell differentiation, apoptosis, transcriptional regulation, and signaling pathways. Here, we show that TRIM15 co-localized to focal adhesions through homo-
PMID 25450970

Targeting the cis-dimerization of LINGO-1 with low MW compounds affects its downstream signalling.

Cobret L1, De Tauzia ML, Ferent J, Traiffort E, Hénaoui I, Godin F, Kellenberger E, Rognan D, Pantel J, Bénédetti H, Morisset-Lopez S.
British journal of pharmacology.Br J Pharmacol.2015 Feb;172(3):841-56. doi: 10.1111/bph.12945. Epub 2014 Dec 15.
BACKGROUND AND PURPOSE: The transmembrane protein LINGO-1 is a negative regulator in the nervous system mainly affecting axonal regeneration, neuronal survival, oligodendrocyte differentiation and myelination. However, the molecular mechanisms regulating its functions are poorly understood. In the p
PMID 25257685

Japanese Journal

マイクロ抗体 : 進化分子工学による分子標的ペプチドの創出

藤井郁雄
有機合成化学協会誌 68(5), 543-550, 2010-05-01
… In both helical regions, uncharged leucine residues were incorporated into the heptad repeat positions to dimerize the α–helices by hydrophobic interactions. …
NAID 10026869196

生物時計による骨格筋機能制御

宮崎充功
体力科學 59(2), 233-242, 2010-04-01
… In mammals, the proteins encoded by Core-Clock genes, Bmal1 and Clock, dimerize to drive transcription of Period and Cryptochrome and the protein products of these genes down-regulate BMAL1 and CLOCK function. …
NAID 10026192046

マイクロ抗体：立体構造規制ペプチド・ライブラリーを用いた分子標的化合物の創出

藤井郁雄
薬学雑誌 129(11), 1303-1309, 2009
… In both helical regions, uncharged leucine residues were incorporated into the heptad repeat positions to dimerize the α-helices by hydrophobic interactions. …
NAID 130000136118