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However, the molecular mechanism of the disease\u2010related mutations affecting the biological function of SNX10 is unclear. Here, we report the crystal structure of human SNX10 to 2.6\u00c5 resolution. The structure reveals that SNX10 contains the extended phox\u2010homology domain we previously proposed. Our study provides the structural details of those disease\u2010related 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\u2013protein interactions. Proteins 2014; 82:3483\u20133489. \u00a9 2014 Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/prot.24689","type":"journal-article","created":{"date-parts":[[2014,9,11]],"date-time":"2014-09-11T14:09:14Z","timestamp":1410444554000},"page":"3483-3489","source":"Crossref","is-referenced-by-count":15,"title":["Structure of human SNX10 reveals insights into its role in human autosomal recessive osteopetrosis"],"prefix":"10.1002","volume":"82","author":[{"given":"Tingting","family":"Xu","sequence":"first","affiliation":[{"name":"State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences Guangzhou 510530 China"},{"name":"School of Life Sciences, University of Science and Technology of China Hefei 230026 China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jinxin","family":"Xu","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and 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