RING finger protein 135 (RNF135, also named Riplet or REUL) exerts multiple biological functions and its C-terminal PRY-SPRY/B30.2 domain is indispensable for most of these functions. RNF135 interacts with RIG-I (retinoic acid-inducible gene-I) via the PRY-SPRY domain and ubiquitinates RIG-I to promote innate anti-viral signaling, while mutations in the RNF135 gene can cause the Macrocephaly, macrosomia, facial dysmorphism (MMFD) syndrome, and RNF135 reportedly regulates the proliferation of glioblastoma cells as well as tongue cancer cells. Nevertheless, structure of full-length RNF135 or its PRY-SPRY domain has not been determined, and structural basis for molecular interactions involving RNF135 is largely unknown. Here we report the backbone ¹H, ¹³C, and ¹⁵N chemical shift assignments of the PRY-SPRY domain of RNF135 and the secondary structure elements predicted based on chemical shifts, as well as the perturbations caused by the R286H mutation that is associated with MMFD syndrome. We found that the mutation did not alter the gross structure of the PRY-SPRY domain, so it may have impaired RNF135 function by affecting protein–protein interactions mediated by the domain.

中文翻译：

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RNF135的PRY-SPRY域的主干1H，13C和15N共振分配。

RING指蛋白135（RNF135，也称为Riplet或REUL）发挥着多种生物学功能，其C端PRY-SPRY / B30.2结构域对于大多数这些功能都是必不可少的。RNF135通过PRY-SPRY结构域与RIG-I（维甲酸诱导的基因-I）相互作用并泛素化RIG-I以促进先天的抗病毒信号传导，而RNF135基因中的突变可引起巨头畸形，巨眼，面部畸形（ MMFD）综合征，据报道，RNF135调节胶质母细胞瘤细胞以及舌头癌细胞的增殖。然而，尚未确定全长RNF135或其PRY-SPRY结构域的结构，并且涉及RNF135的分子相互作用的结构基础在很大程度上是未知的。在这里，我们报告主干¹ H，¹³ C和¹⁵NNF135的PRY-SPRY域的N个化学位移分配和基于化学位移以及与MMFD综合征相关的R286H突变引起的扰动预测的二级结构元素。我们发现该突变不会改变PRY-SPRY结构域的总体结构，因此它可能通过影响该结构域介导的蛋白质间相互作用而损害RNF135功能。