 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](pg5092fig1mag.jpg)
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Figure 1
(a) A schematic of NPC1 showing the 13 transmembrane domains (1–13), luminal domains A, C and I and the sterol-sensing domain (SSD). (b) Ni–NTA affinity-purified His8-tagged NPC1-C was refolded and purified to homogeneity using size-exclusion chromatography. A representative Superdex 200 16/60 gel-filtration profile of the refolded protein is shown. The expected molecular weight of NPC1-C is 30 kDa. The inset shows SDS–PAGE profiles of the final purified protein taken from the labeled peak and prepared under nonreducing (β-me −) and reducing (β-me +) buffer conditions. (c) Cartoon representation of an NPC1-C monomer, rainbow-colored from the N-terminus (blue) to the C-terminus (red), with the seven predicted N-linked glycosylation sites (Asn452, Asn459, Asn478, Asn524, Asn557, Asn572 and Asn598) indicated as spheres. The dashed lines indicate linker segments between NPC1-C and transmembrane domains 2 and 3 (TM2 and TM3). (d) Antiparallel dimer in the asymmetric unit. |
![[Figure 1]](pg5092fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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