8BLP
Human Urea Transporter UT-B/UT1 in Complex with Inhibitor UTBinh-14
Summary for 8BLP
| Entry DOI | 10.2210/pdb8blp/pdb |
| EMDB information | 16110 16111 16112 |
| Descriptor | Urea transporter 1, PHOSPHATIDYLETHANOLAMINE, DODECYL-BETA-D-MALTOSIDE, ... (6 entities in total) |
| Functional Keywords | slc14a1, ut1, ut-b, urea transporter, inhibitor, solute carrier, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 155171.46 |
| Authors | Chi, G.,Dietz, L.,Pike, A.C.W.,Maclean, E.M.,Mukhopadhyay, S.M.M.,Bohstedt, T.,Wang, D.,Scacioc, A.,McKinley, G.,Arrowsmith, C.H.,Edwards, A.,Bountra, C.,Fernandez-Cid, A.,Burgess-Brown, N.A.,Duerr, K.L. (deposition date: 2022-11-10, release date: 2023-10-04, Last modification date: 2023-10-11) |
| Primary citation | Chi, G.,Dietz, L.,Tang, H.,Snee, M.,Scacioc, A.,Wang, D.,Mckinley, G.,Mukhopadhyay, S.M.M.,Pike, A.C.W.,Chalk, R.,Burgess-Brown, N.A.,Timmermans, J.P.,van Putte, W.,Robinson, C.V.,Durr, K.L. Structural characterization of human urea transporters UT-A and UT-B and their inhibition. Sci Adv, 9:eadg8229-eadg8229, 2023 Cited by PubMed Abstract: In this study, we present the structures of human urea transporters UT-A and UT-B to characterize them at molecular level and to detail the mechanism of UT-B inhibition by its selective inhibitor, UTB-14. High-resolution structures of both transporters establish the structural basis for the inhibitor's selectivity to UT-B, and the identification of multiple binding sites for the inhibitor will aid with the development of drug lead molecules targeting both transporters. Our study also discovers phospholipids associating with the urea transporters by combining structural observations, native MS, and lipidomics analysis. These insights improve our understanding of urea transporter function at a molecular level and provide a blueprint for a structure-guided design of therapeutics targeting these transporters. PubMed: 37774028DOI: 10.1126/sciadv.adg8229 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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