Bashir Samirul, Pal Debnath, Qadri Ozaira, Banday Mariam, Fazili Khalid
University of Kashmir, Srinagar, Jammu and Kashmir, India.
Indian Institute of Science Bangalore, Bengaluru, Karnataka, India.
MicroPubl Biol. 2023 Mar 28;2023. doi: 10.17912/micropub.biology.000763. eCollection 2023.
IRE1 belongs to a type I transmembrane protein family harboring two functional domains, cytoplasmic domain with kinase and RNAse catalytic activity, and the luminal domain, which is involved in the sensing of unfolded proteins. IRE1 molecule undergoes dimerization in the lumenal domain, which functionally activates the catalytic C-terminal domain. IRE1 activation is directly related to transition between monomeric and dimeric forms. We have deduced two quaternary structures from the published crystal structure of IRE1. One structure with a large stable interface that requires large activation and deactivation energy to active IRE1. The other quaternary structure has low dissociation energy and is more suitable for IRE1 oligomeric transition.
肌醇需求酶1（IRE1）属于I型跨膜蛋白家族，具有两个功能结构域，即具有激酶和核糖核酸酶催化活性的胞质结构域以及参与未折叠蛋白感知的腔结构域。IRE1分子在腔结构域中发生二聚化，从而在功能上激活催化性的C末端结构域。IRE1的激活与单体形式和二聚体形式之间的转变直接相关。我们根据已发表的IRE1晶体结构推导了两种四级结构。一种结构具有大的稳定界面，激活IRE1需要大量的激活和失活能量。另一种四级结构具有低解离能，更适合IRE1的寡聚体转变。
