- 著者
-
禾 晃和
- 出版者
- 日本結晶学会
- 雑誌
- 日本結晶学会誌 (ISSN:03694585)
- 巻号頁・発行日
- vol.64, no.4, pp.269-278, 2022-12-15 (Released:2022-12-17)
- 参考文献数
- 40
Protein-protein interactions are essential in diverse cellular processes including signal transduction. It is not uncommon for protein-protein interactions in the transmembrane signaling to exhibit low binding affinities with a dissociation constant in the μM range or higher. Presumably, membrane proteins can selectively bind with their binding partners via low-affinity interactions because they can only diffuse laterally in the membrane plane and interact with the partners within a limited space on the membrane surface or within the membrane. This review focuses on the crystallographic studies on cell-surface receptors and intramembrane proteases that perform the transmembrane signaling mediated by low-affinity protein-protein interactions.