生体膜上で形成される低親和性タンパク質間相互作用の構造生物学的研究

抄録

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.