Protein dimer
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 (process called homodimerization). A hetero-dimer would be formed by two different macromolecules (process 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
- 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
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.
- ^ 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.
See also [edit]
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