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Updated: Jan 22, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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細胞内陽性アロステル調節器によるβ2AR調節のメカニズム

Xiangyu Liu1, Ali Masoudi2, Alem W Kahsai2

  • 1Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.

Science (New York, N.Y.)
|June 29, 2019
PubMed
まとめ

研究者らは,陽性アロステル調節器に結合したGタンパク質結合受容体の構造を明らかにした. これは,アロステリック薬が治療上の利益のために受容体の形状を安定させる方法を示しています.

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Allosteric Regulation01:08

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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