Structure of human SNX10 reveals insights into its role in human autosomal recessive osteopetrosis

• DOI: 10.1002/prot.24689
• Publication Date: 2014-09-11T14:09:14Z
• Authors: Tingting Xu; Jinxin Xu; Yinghua Ye; Qi Wang; Xiaodong Shu; Duanqing Pei; Jinsong Liu
• Keywords: Sorting nexin; Osteopetrosis

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