- 関
- heterodimerize
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/07/14 14:29:55」(JST)
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"Dimerize" redirects here. For other uses, see Dimer.
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.
See also
- Dimer (chemistry)
- Protein trimer
- Oligomer
- ProtCID
- Molecular and cellular biology portal
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English Journal
- Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
- Shalom-Elazari H1, Zazrin-Greenspon H1, Shaked H1, Chill JH2.
- Biochimica et biophysica acta.Biochim Biophys Acta.2014 Nov;1838(11):2919-28. doi: 10.1016/j.bbamem.2014.07.023. Epub 2014 Aug 7.
- E1 and E2 are two hepatitis C viral envelope glycoproteins that assemble into a heterodimer that is essential for membrane fusion and penetration into the target cell. Both extracellular and transmembrane (TM) glycoprotein domains contribute to this interaction, but study of TM-TM interactions has b
- PMID 25109935
- Targeting HER3 with miR-450b-3p suppresses breast cancer cells proliferation.
- Zhao Z1, Li R2, Sha S1, Wang Q1, Mao W1, Liu T1.
- Cancer biology & therapy.Cancer Biol Ther.2014 Oct 1;15(10):1404-12. doi: 10.4161/cbt.29923. Epub 2014 Jul 21.
- In breast cancer cells, heterodimerization of HER2 and HER3 plays important and dominant roles in the functionality and transformation of HER-mediated pathways, in particular the PI3K/Akt survival pathway. HER3 was considered as a major signaling hub in HER2-amplified cancers. Inhibition of HER3 exp
- PMID 25046105
- Conditional targeting of MAD1 to kinetochores is sufficient to reactivate the spindle assembly checkpoint in metaphase.
- Kuijt TE1, Omerzu M, Saurin AT, Kops GJ.
- Chromosoma.Chromosoma.2014 Oct;123(5):471-80. doi: 10.1007/s00412-014-0458-9. Epub 2014 Apr 4.
- Fidelity of chromosome segregation is monitored by the spindle assembly checkpoint (SAC). Key components of the SAC include MAD1, MAD2, BUB1, BUB3, BUBR1, and MPS1. These proteins accumulate on kinetochores in early prometaphase but are displaced when chromosomes attach to microtubules and/or biorie
- PMID 24695965
Japanese Journal
- ヘテロダイマー形成によるホヤGnRH受容体パラログのdifferentialな機能調節機構
- μ-Opioid Receptor Forms a Functional Heterodimer With Cannabinoid CB_1 Receptor : Electrophysiological and FRET Assay Analysis
- HOJO Minoru,SUDO Yuka,ANDO Yuko,MINAMI Koichiro,TAKADA Masafumi,MATSUBARA Takehiro,KANAIDE Masato,TANIYAMA Kohtaro,SUMIKAWA Koji,UEZONO Yasuhito
- Journal of pharmacological sciences 108(3), 308-319, 2008-11-20
- … Experiments with endogenous Gi/o protein inactivation by pertussis toxin (PTX) supported the functional heterodimerization of μOR/CB1R through PTX-insensitive Gqi5(m) fused to each receptor. …
- NAID 10024593115
- Early sexual origins of homeoprotein heterodimerization and evolution of the plant KNOX/BELL family
Related Links
- Definition of heterodimerization in the Definitions.net dictionary. Meaning of heterodimerization. What does heterodimerization mean? Information and translations of heterodimerization in the most comprehensive dictionary definitions ...
- Looking for online definition of Heterodimerization in the Medical Dictionary? Heterodimerization explanation free. What is Heterodimerization? Meaning of Heterodimerization medical term. What does Heterodimerization mean? ...
Related Pictures
★リンクテーブル★
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- 英
- heterodimerization、heterodimerize
- 関
- ヘテロ二量体形成
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- 関
- heterodimerization
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- 英
- heterodimerization
- 関
- ヘテロ二量体化