Sterol-sensing domain

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]

Function

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:

Disease

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]

See also

References

  1. "Sterol-sensing domain". InterPro. European Bioinformatics Institute. Retrieved 25 March 2015.
  2. Kuwabara, PE; Labouesse, M (April 2002). "The sterol-sensing domain: multiple families, a unique role?". Trends in Genetics 18 (4): 193–201. doi:10.1016/s0168-9525(02)02640-9. PMID 11932020.
  3. Pasca di Magliano, M; Hebrok, M (December 2003). "Hedgehog signalling in cancer formation and maintenance.". Nature reviews. Cancer 3 (12): 903–11. doi:10.1038/nrc1229. PMID 14737121.
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