Oxysterol-binding protein
| Oxysterol-binding protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystallographic structure of the oxysterol-binding protein (rainbow color cartoon, N-terminus = blue, C-terminus = red) bound to 7-hydroxycholesterol (stick diagram, carbon = white, oxygen = red).[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Oxysterol_BP | ||||||||
| Pfam | PF01237 | ||||||||
| InterPro | IPR000648 | ||||||||
| PROSITE | PDOC00774 | ||||||||
| OPM superfamily | 173 | ||||||||
| OPM protein | 1zi7 | ||||||||
| |||||||||
Oxysterol-binding proteins, or Oxysterol-binding protein related-proteins, or simply ORPs, are evolutionary related proteins involved in sterol synthesis and/or its regulation.[2] These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds oxysterols (oxygenated derivatives of cholesterol), cholesterol and phosphatidylinositol 4-phosphate (PI4P); yeast Osh1, a protein of 859 residues that plays a role in ergosterol synthesis; and yeast proteins HES1 and KES1, highly related proteins of 434 residues that seem to play a role in ergosterol synthesis[3]
References
- ↑ Im, Y. J.; Raychaudhuri, S.; Prinz, W. A.; Hurley, J. H. (2005). "Structural mechanism for sterol sensing and transport by OSBP-related proteins". Nature 437 (7055): 154–158. doi:10.1038/nature03923. PMC 1431608. PMID 16136145. PDB 1ZHT; Im, Y. J.; Raychaudhuri, S.; Prinz, W. A.; Hurley, J. H. (2005). Structure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol. doi:10.2210/pdb1zht/pdb.
- ↑ Jiang, B.; Brown, J. L.; Sheraton, J.; Fortin, N.; Bussey, H. (1994). "A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein". Yeast 10 (3): 341–353. doi:10.1002/yea.320100307. PMID 8017104.
- ↑ Li, X.; Rivas, M. P.; Fang, M.; Marchena, J.; Mehrotra, B.; Chaudhary, A.; Feng, L.; Prestwich, G. D.; Bankaitis, V. A. (2002). "Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex". The Journal of Cell Biology 157 (1): 63–77. doi:10.1083/jcb.200201037. PMC 2173257. PMID 11916983.
Human proteins from this family
OBPH1; OSBP; OSBP2; OSBPL10; OSBPL11; OSBPL1A; OSBPL2; OSBPL3; OSBPL5; OSBPL6; OSBPL7; OSBPL8; OSBPL9;
This article incorporates text from the public domain Pfam and InterPro IPR000648