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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 like proteins or nucleic acids. It is a quaternary structure of a protein.

A homo-dimer would be formed by two identical molecules (a process called homodimerization). A hetero-dimer would be formed by two different macromolecules (called heterodimerization).

Most dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer would be 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[edit]

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[edit]

^ 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. Cite uses deprecated parameters (help)
^ 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". Biochem. Biophys. Res. Commun. 367 (1): 103–8. doi:10.1016/j.bbrc.2007.12.123. PMC 2277332. PMID 18164680. Cite uses deprecated parameters (help)

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English Journal

Regulation of the System x(-) (C) cystine/glutamate exchanger by intracellular glutathione levels in rat astrocyte primary cultures.

Seib TM, Patel SA, Bridges RJ.SourceCSFN, Center for Structural and Functional Neuroscience, Department of Biomedical and Pharmaceutical Sciences, University of Montana, Missoula, Montana.
Glia.Glia.2011 Oct;59(10):1387-401. doi: 10.1002/glia.21176. Epub 2011 May 17.
The system x?C- (Sx?C-) transporter functions to mediate the exchange of extracellular cystine (L-Cys(2) ) and intracellular glutamate (L-Glu). Internalized L-Cys(2) serves as a rate-limiting precursor for the biosynthesis of glutathione (GSH), while the externalized L-Glu can contribute to eith
PMID 21590811

Purification and partial characterization of a novel phosphodiesterase from the venom of Trimeresurus stejnegeri: Inhibition of platelet aggregation.

Peng L, Xu X, Shen D, Zhang Y, Song J, Yan X, Guo M.SourceDepartment of Chemistry, University of Science and Technology of China, No. 96, Jinzhai Road, Hefei, Anhui 230026, PR China.
Biochimie.Biochimie.2011 Sep;93(9):1601-9. Epub 2011 Jun 1.
The phosphodiesterases (PDEs) are a superfamily of enzymes that have multiple roles in extracellular nucleotide metabolism and in the regulation of nucleotide-based intercellular signaling. Here we describe for the first time the isolation and partial characterization of a novel phosphodiesterase fr
PMID 21664407

Japanese Journal

Enhancing recombinant protein production in human cell lines with a constitutive transport element and mRNA export proteins.

Aihara Yuki,Fujiwara Naoko,Yamazaki Tomohiro,Kambe Taiho,Nagao Masaya,Hirose Yutaka,Masuda Seiji
Journal of biotechnology 153(3-4), 86-91, 2011-05-20
… Among them, the Tap-p15 heterodimer acts as an mRNA export receptor. …
NAID 120003072129

Involvement of SLX4 in interstrand cross-link repair is regulated by the Fanconi anemia pathway.

Yamamoto Kimiyo N,Kobayashi Shunsuke,Tsuda Masataka,Kurumizaka Hitoshi,Takata Minoru,Kono Koichi,Takeda Shunichi,Hirota Kouji
Proceedings of the National Academy of Sciences of the United States of America 108(16), 6492-6496, 2011-04-19
… Once it is posttranslationally modified, this heterodimer recruits downstream members of the ICL repairosome, including the FAN1 nuclease. …
NAID 120003072120