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From Wikipedia, the free encyclopedia
A sterol-sensing domain (SSD) is a protein domain which consists of 180 amino acids forming five transmembrane segments capable of binding sterol groups. This type of domain is present in proteins involved in cholesterol metabolism and signalling.[1]
Sterol-sensing domains are present in various proteins involved in key aspects of cholesterol homeostasis and signalling. Multiple sequence alignments using Clustal W have shown that these proteins can be grouped in seven different families according to their SSDs.[2] The following SSD-containing proteins represent each family:
Mutations in 7DHCR are linked to Smith–Lemli–Opitz syndrome (SLOS). Mutations in NPC1 have been shown to cause Niemann–Pick disease, type C. Mutations in patched are associated with a variety of cancers (basal cell carcinoma, medulloblastoma, rhabdomyosarcoma).[3]
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