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Aug 11, 2005 · Protein subunit interaction (either homodimer or heterodimer) is an important phenomenon in regulation and catalysis. Thousands of such interactions are theoretically possible in a combinatorial manner. The task of documenting each of these interactions is laborious.
- Cui Zhanhua, Jacob Gah-Kok Gan, Li lei, Meena Kishore Sakharkar, Pandjassarame Kangueane
- 10.6026/97320630001028
- 2005
- Bioinformation. 2005; 1(2): 28-39.
The interaction between the subunits is often mediated by non-covalent bonds, such as hydrogen bonds, electrostatic interactions, and hydrophobic interactions. Heterodimers can exhibit unique properties compared to their individual subunits, allowing for increased functional diversity.
Proteins form homo-, hetero-, or oligomerization in the cellular environment to regulate the cellular processes. Any deregulation of these processes may result in a disease state. Protein–protein interactions (PPIs) can be inhibited by antibodies, small molecules, or peptides, and inhibition of PPI has therapeutic value.
- Sitanshu S. Singh, Seetharama D. Jois
- 10.1016/bs.apcsb.2017.08.003
- 2018
- 2018
Nov 5, 2019 · We show that heterodimers can be thought of as molecular devices through which precise control of gene transcription can be achieved by using combinatorial sets of ligands, thereby allowing for the initiation of complex gene programs in a cell-specific manner.
- Albane Le Maire, Catherine Teyssier, Patrick Balaguer, William Bourguet, Pierre Germain
- 10.3390/cells8111392
- 2019
- Cells. 2019 Nov; 8(11): 1392.
Oct 13, 2022 · Many chemokines engage in heterophilic interactions to form heterodimers, leading to synergistic activity enhancement or reduction dependent on the nature of heterodimer-forming chemokines.
The formation of heterodimers between GFP- and S549-labeled constructs should ideally result in the appearance of diffusing fluorescent spots at the plasma membrane that emit light in both the green and the red channel (referred to as yellow spots hereafter).
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Dec 13, 2023 · We propose that the glycine-rich nature of the mGluR4 cysteine loop renders it more flexible than the mGluR7 loop, reducing its ability to cooperatively interact with the loop on the partner...
