4ON3

Crystal structure of human sorting nexin 10 (SNX10)

4ON3 の概要

• エントリーDOI: 10.2210/pdb4on3/pdb
• 分子名称: Sorting nexin-10, NITRATE ION, PENTAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: sorting nexin, phox-homology domain, protein transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: Q9Y5X0
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52773.61

構造登録者

Xu, T.,Xu, J.,Wang, Q.,Liu, J. (登録日: 2014-01-28, 公開日: 2014-09-24, 最終更新日: 2024-11-06)

主引用文献

Xu, T.,Xu, J.,Ye, Y.,Wang, Q.,Shu, X.,Pei, D.,Liu, J.
Structure of human SNX10 reveals insights into its role in human autosomal recessive osteopetrosis.
Proteins, 82:3483-3489, 2014

PubMed Abstract: Sorting nexin 10 (SNX10), the unique member of the SNX family having vacuolation activity in cells, was shown to be involved in the development of autosomal recessive osteopetrosis (ARO) in recent genetic studies. However, the molecular mechanism of the disease-related mutations affecting the biological function of SNX10 is unclear. Here, we report the crystal structure of human SNX10 to 2.6 Å resolution. The structure reveals that SNX10 contains the extended phox-homology domain we previously proposed. Our study provides the structural details of those disease-related mutations. Combined with the vacuolation study of those mutations, we found that Tyr32 and Arg51 are important for the protein stability and both play a critical role in vacuolation activity, while Arg16Leu may affect the function of SNX10 in osteoclast through protein-protein interactions.

PubMed: 25212774
DOI: 10.1002/prot.24689

実験手法

X-RAY DIFFRACTION (2.6 Å)