Oxysterol-binding protein

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Oxysterol-binding protein
Identifiers
Symbol Oxysterol_BP
Pfam PF01237
InterPro IPR000648
PROSITE PDOC00774
OPM protein 1zi7
Available PDB structures:

1zhtA:2-424 1zi7A:30-424 1zhzA:2-424 1zhwA:2-424 1zhyA:2-424 1zhxA:2-424

Oxysterol-binding proteins are evolutionary related proteins involved with sterol synthesis and/or its regulation [1]. These include mammalian oxysterol-binding protein (OSBP), a protein of about 800 amino-acid residues that binds a variety of oxysterols (oxygenated derivatives of cholesterol); yeast OSH1, a protein of 859 residues that also 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[2]

[edit] References

  1. ^ Bussey H, Fortin N, Jiang B, Brown JL, Sheraton J (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. 
  2. ^ Analysis of oxysterol binding protein homologue Kes1p function in regulation of Sec14p-dependent protein transport from the yeast Golgi complex. Li X, Rivas MP, Fang M, Marchena J, Mehrotra B, Chaudhary A, Feng L, Prestwich GD, Bankaitis VA; J Cell Biol 2002;157:63-77. PubMed

[edit] Human proteins containing this domain

OBPH1; OSBP; OSBP2; OSBPL10; OSBPL11; OSBPL1A; OSBPL2; OSBPL3; OSBPL5; OSBPL6; OSBPL7; OSBPL8; OSBPL9;

This article includes text from the public domain Pfam and InterPro IPR000648

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