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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ye, Yinghua Pei, Duanqing Wu, Bin Xu, Tingting Shu, Xiaodong Liu, Jinsong You, Xiaojuan Xu, Jinxin |
| Description | Author Affiliation: Xu J ( State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.) |
| Abstract | Sorting nexins are phox homology (PX) domain-containing proteins involved in diverse intracellular endosomal trafficking pathways. The PX domain binds to certain phosphatidylinositols and is recruited to vesicles rich in these lipids. The structure of the PX domain is highly conserved, containing a three-stranded ß-sheet, followed by three -helices. Here, we report the crystal structures of truncated human SNX11 (sorting nexin 11). The structures reveal that SNX11 contains a novel PX domain, hereby named the extended PX (PXe) domain, with two additional -helices at the C terminus. We demonstrate that these -helices are indispensible for the in vitro functions of SNX11. We propose that this PXe domain is present in SNX10 and is responsible for the vacuolation activity of SNX10. Thus, this novel PXe domain constitutes a structurally and functionally important PX domain subfamily. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 23 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-06-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Sorting Nexins Chemistry Vacuoles Phosphatidylinositols Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Genetics Metabolism Structure-Activity Relationship Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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