Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage [1,2]. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1 [4,5]. [1]. 9013611. Molecular identification of a novel candidate sorting receptor. purified from human brain by receptor-associated protein. affinity chromatography.. Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N,. Rasmussen HH, Roigaard H, Gliemann J, Madsen P, Moestrup SK;. J Biol Chem. 1997;272:3599-3605.. [2]. 9756851. The 100-kDa neurotensin receptor is gp95/sortilin, a. non-G-protein-coupled receptor.. Mazella J, Zsurger N, Navarro V, Chabry J, Kaghad M, Caput D,. Ferrara P, Vita N, Gully D, Maffrand JP, Vincent JP;. J Biol Chem. 1998;273:26273-26276.. [3]. 10085125. Sortilin/neurotensin receptor-3 binds and mediates degradation. of lipoprotein lipase.. Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM;. J Biol Chem. 1999;274:8832-8836.. [4]. 19122660. Ligands bind to Sortilin in the tunnel of a ten-bladed. beta-propeller domain.. Quistgaard EM, Madsen P, Groftehauge MK, Nissen P, Petersen C. TRUNCATED at 1650 bytes (from Pfam)
- Date:
- 2024-08-14