5XQI

Crystal structure of full-length human Rogdi

5XQI の概要

• エントリーDOI: 10.2210/pdb5xqi/pdb
• 分子名称: Protein rogdi homolog (2 entities in total)
• 機能のキーワード: rogdi, kohlschutter-tonz syndrome, cell cycle
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Nucleus envelope : Q9GZN7
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 129736.99

構造登録者

Lee, H.,Lee, C. (登録日: 2017-06-07, 公開日: 2017-07-12, 最終更新日: 2023-11-22)

主引用文献

Lee, H.,Jeong, H.,Choe, J.,Jun, Y.,Lim, C.,Lee, C.
The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tonz Syndrome
Sci Rep, 7:3972-3972, 2017

PubMed Abstract: Kohlschutter-Tönz syndrome (KTS) is a rare autosomal-recessive disorder of childhood onset characterized by global developmental delay, spasticity, epilepsy, and amelogenesis imperfecta. Rogdi, an essential protein, is highly conserved across metazoans, and mutations in Rogdi are linked to KTS. However, how certain mutations in Rogdi abolish its physiological functions and cause KTS is not known. In this study, we determined the crystal structure of human Rogdi protein at atomic resolution. Rogdi forms a novel elongated curved structure comprising the α domain, a leucine-zipper-like four-helix bundle, and a characteristic β-sheet domain. Within the α domain, the N-terminal H1 helix (residues 19-45) pairs with the C-terminal H6 helix (residues 252-287) in an antiparallel manner, indicating that the integrity of the four-helix bundle requires both N- and C-terminal residues. The crystal structure, in conjunction with biochemical data, indicates that the α domain might undergo a conformational change and provide a structural platform for protein-protein interactions. Disruption of the four-helix bundle by mutation results in significant destabilization of the structure. This study provides structural insights into how certain mutations in Rogdi affect its structure and cause KTS, which has important implications for the development of pharmaceutical agents against this debilitating neurological disease.

PubMed: 28638151
DOI: 10.1038/s41598-017-04120-x

実験手法

X-RAY DIFFRACTION (2.8 Å)