In organic chemistry, atoms other than carbon and hydrogen are generally referred to as heteroatoms. The most common heteroatoms are nitrogen, oxygen and sulfur. Now I present to you an article called Structural basis for itraconazole-mediated NPC1 inhibition, published in 2020-12-31, which mentions a compound: 16588-26-4, mainly applied to ovarian cell NPC1 itraconazole sterol sensing domain cholesterol, Recommanded Product: 3-Bromo-4-chloronitrobenzene.
Niemann-Pick C1, a lysosomal protein of 13 transmembrane helixes and three lumenal domains, exports low-d.-lipoprotein-derived cholesterol from lysosomes. TMs 3-7 of NPC1 comprise the sterol-sensing domain. Previous studies suggest that mutation of the NPC1-SSD or the addition of the anti-fungal drug itraconazole abolishes NPC1 activity in cells. However, the itraconazole binding site and the mechanism of NPC1-mediated cholesterol transport remain unknown. Here, we report a cryo-EM structure of human NPC1 bound to itraconazole, which reveals how this binding site in the center of NPC1 blocks a putative lumenal tunnel linked to the SSD. Functional assays confirm that blocking this tunnel abolishes NPC1-mediated cholesterol egress. Intriguingly, the palmitate anchor of Hedgehog occupies a similar site in the homologous tunnel of Patched, suggesting a conserved mechanism for sterol transport in this family of proteins and establishing a central function of their SSDs.
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