放射毒素
FERM功能域
埃兹林
反平行(数学)
莫辛
七肽重复区
生物物理学
螺旋线圈
二聚体
结晶学
蛋白质结构
细胞骨架
生物
化学
膜蛋白
肽序列
膜
生物化学
物理
整体膜蛋白
有机化学
细胞
量子力学
磁场
基因
作者
Juanita M. Phang,S.J. Harrop,Anthony P. Duff,Anna Sokolova,Ben Crossett,James Walsh,Simone A. Beckham,Cuong D. Nguyen,Roberta B. Davies,Carina Glöckner,Elizabeth H. C. Bromley,Krystyna E. Wilk,Paul M. G. Curmi
摘要
Ezrin is a member of the ERM (ezrin–radixin–moesin) family of proteins that have been conserved through metazoan evolution. These proteins have dormant and active forms, where the latter links the actin cytoskeleton to membranes. ERM proteins have three domains: an N-terminal FERM [band Four-point-one (4.1) ERM] domain comprising three subdomains (F1, F2, and F3); a helical domain; and a C-terminal actin-binding domain. In the dormant form, FERM and C-terminal domains form a stable complex. We have determined crystal structures of the active FERM domain and the dormant FERM:C-terminal domain complex of human ezrin. We observe a bistable array of phenylalanine residues in the core of subdomain F3 that is mobile in the active form and locked in the dormant form. As subdomain F3 is pivotal in binding membrane proteins and phospholipids, these transitions may facilitate activation and signaling. Full-length ezrin forms stable monomers and dimers. We used small-angle X-ray scattering to determine the solution structures of these species. As expected, the monomer shows a globular domain with a protruding helical coiled coil. The dimer shows an elongated dumbbell structure that is twice as long as the monomer. By aligning ERM sequences spanning metazoan evolution, we show that the central helical region is conserved, preserving the heptad repeat. Using this, we have built a dimer model where each monomer forms half of an elongated antiparallel coiled coil with domain-swapped FERM:C-terminal domain complexes at each end. The model suggests that ERM dimers may bind to actin in a parallel fashion.
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