4PZG

Crystal structure of human sorting nexin 10 (SNX10)

Summary for 4PZG

• Entry DOI: 10.2210/pdb4pzg/pdb
• Related: 4ON3
• Descriptor: Sorting nexin-10, NITRATE ION, 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL, ... (4 entities in total)
• Functional Keywords: sorting nexin, protein transport, phox-homology domain
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q9Y5X0
• Total number of polymer chains: 2
• Total formula weight: 52874.45

Authors

Xu, T.,Xu, J.,Wang, Q.,Liu, J. (deposition date: 2014-03-30, release date: 2014-09-24, Last modification date: 2014-12-03)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)