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- heterodimerization
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/07/07 12:44:08」(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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UpToDate Contents
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English Journal
- Homodimerization of the Wnt Receptor DERAILED Recruits the Src Family Kinase SRC64B.
- Petrova IM, Lahaye LL, Martiáñez T, de Jong AW, Malessy MJ, Verhaagen J, Noordermeer JN, Fradkin LG.SourceLaboratory of Developmental Neurobiology, Department of Molecular Cell Biology, Leiden University Medical Center, 2300 RC Leiden, The Netherlands.
- Molecular and cellular biology.Mol Cell Biol.2013 Aug 26. [Epub ahead of print]
- Ryk pseudokinase receptors act as important transducers of Wnt signals particularly in the nervous system. Little is known, however, of their interactions at the cell surface. Here, we show that a Drosophila Ryk family member, DERAILED, forms cell surface homodimers and can also heterodimerize with
- PMID 23979591
- Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5.
- Ni L, Li S, Yu J, Min J, Brautigam CA, Tomchick DR, Pan D, Luo X.SourceDepartment of Pharmacology, The University of Texas Southwestern Medical Center, 6001 Forest Park Road, Dallas, TX 75390, USA.
- Structure (London, England : 1993).Structure.2013 Aug 20. pii: S0969-2126(13)00258-X. doi: 10.1016/j.str.2013.07.008. [Epub ahead of print]
- The tumor-suppressive Hippo pathway controls tissue homeostasis through balancing cell proliferation and apoptosis. Activation of the kinases Mst1 and Mst2 (Mst1/2) is a key upstream event in this pathway and remains poorly understood. Mst1/2 and their critical regulators RASSFs contain Salvador/RAS
- PMID 23972470
- Isolation and Characterization of Mutant Sinorhizobium meliloti NodD1 Proteins with Altered Responses to Luteolin.
- Peck MC, Fisher RF, Bliss R, Long SR.SourceDepartment of Medicine, Division of Infectious Diseases, University of California, San Francisco, California, USA.
- Journal of bacteriology.J Bacteriol.2013 Aug;195(16):3714-23. doi: 10.1128/JB.00309-13. Epub 2013 Jun 14.
- NodD1, a member of the NodD family of LysR-type transcriptional regulators (LTTRs), mediates nodulation (nod) gene expression in the soil bacterium Sinorhizobium meliloti in response to the plant-secreted flavonoid luteolin. We used genetic screens and targeted approaches to identify NodD1 residues
- PMID 23772067
Japanese Journal
- Decreased expression of retinoid X receptor isoforms in human thyroid carcinomas
- 滝山 由美,Miyokawa N,Sugawara A,Kato S,Ito K,Sato K,Oikawa K,Kobayashi H,Kimura S,Tateno H
- Journal of Clinical Endocrinology & Metabolism 89(11), 5851-5861, 2004-11
- … Because RXRs heterodimerize with thyroid hormone receptor, retinoic acid receptor, vitamin D(3) receptor, and peroxisome proliferator-activated receptor, they play central roles in regulating a number of signaling pathways. …
- NAID 120003161786
- Transforming growth factor-beta-stimulated clone-22 is a member of a family of leucine zipper proteins that can homo- and heterodimerize and has transcriptional repressor activity
- Two domains unique to osteoblast-specific transcription factor Osf2/Cbfal contribute to its transcription function and its inability to heterodimerize with Cbfβ.
Related Links
- When PER and CRY proteins accumulate in the cytosol, they heterodimerize and translocate to the nucleus where they act as transcriptional repressors to terminate CLOCK-BMALl-mediated transcription, thus ending the molecular ...
- Definition and other additional information on Heterodimerize from Biology-Online.org dictionary. Login Welcome to biology-online.org! Please login to access all site features. Create account. Log me on automatically each visit | ...
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