8EUS
Crystal structure of NPC1 luminal domain C
Summary for 8EUS
| Entry DOI | 10.2210/pdb8eus/pdb |
| Descriptor | NPC intracellular cholesterol transporter 1 (2 entities in total) |
| Functional Keywords | niemann pick, luminal domain, cholesterol, ebola, virus entry, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 60334.91 |
| Authors | Odongo, L.,Pornillos, O. (deposition date: 2022-10-19, release date: 2023-02-22, Last modification date: 2024-10-23) |
| Primary citation | Odongo, L.,Zadrozny, K.K.,Diehl, W.E.,Luban, J.,White, J.M.,Ganser-Pornillos, B.K.,Tamm, L.K.,Pornillos, O. Purification and structure of luminal domain C of human Niemann-Pick C1 protein. Acta Crystallogr.,Sect.F, 79:45-50, 2023 Cited by PubMed Abstract: Niemann-Pick C1 protein (NPC1) is a membrane protein that primarily resides in late endosomes and lysosomes, and plays an important role in cholesterol homeostasis in the cell. The second luminal domain of NPC1 (NPC1-C) serves as the intracellular receptor for Ebola and Marburg viruses. Here, the recombinant production of nonglycosylated and glycosylated NPC1-C and a new crystal form of the nonglycosylated protein are reported. The crystals belonged to space group P2 and diffracted to 2.3 Å resolution. The structure is similar to other reported structures of NPC1-C, with differences observed in the protruding loops when compared with NPC1-C in complex with Ebola virus glycoprotein or NPC2. PubMed: 36748341DOI: 10.1107/S2053230X23000705 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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