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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/01/09 19:29:35」(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. (The word dimer has roots meaning "two parts", di- + -mer.) 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
Tubulin

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

Decreased homodimerization and increased TIMP-1 complexation of uteroplacental and uterine arterial matrix metalloproteinase-9 during hypertension-in-pregnancy.

Chen J1, Ren Z1, Zhu M1, Khalil RA2.
Biochemical pharmacology.Biochem Pharmacol.2017 Aug 15;138:81-95. doi: 10.1016/j.bcp.2017.05.005. Epub 2017 May 12.
PMID 28506758

Structure of the C-terminal domain of TRADD reveals a novel fold in the death domain superfamily.

Zhang N1, Yuan W1, Fan JS2, Lin Z3,4,5.
Scientific reports.Sci Rep.2017 Aug 1;7(1):7073. doi: 10.1038/s41598-017-07348-9.
PMID 28765645

Target specificity, in vivo pharmacokinetics, and efficacy of the putative STAT3 inhibitor LY5 in osteosarcoma, Ewing's sarcoma, and rhabdomyosarcoma.

Yu PY1, Gardner HL2, Roberts R3, Cam H3, Hariharan S4, Ren L5, LeBlanc AK5, Xiao H3, Lin J3, Guttridge DC6,7, Mo X8, Bennett CE9, Coss CC10, Ling Y10, Phelps MA10, Houghton P4, London CA2,11.
PloS one.PLoS One.2017 Jul 27;12(7):e0181885. doi: 10.1371/journal.pone.0181885. eCollection 2017.
PMID 28750090