Oxysterol-binding protein homolog

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Revision as of 13:17, 29 November 2018

Yeast oxysterol-binding protein homolog 4 complex with cholesterol and Pb+2 ion (black) (PDB code 1zhy)

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Updated on 29-November-2018

↑ Tian S, Ohta A, Horiuchi H, Fukuda R. Oxysterol-binding protein homologs mediate sterol transport from the endoplasmic reticulum to mitochondria in yeast. J Biol Chem. 2018 Apr 13;293(15):5636-5648. doi: 10.1074/jbc.RA117.000596. Epub, 2018 Feb 27. PMID:29487131 doi:http://dx.doi.org/10.1074/jbc.RA117.000596
↑ Mousley CJ, Yuan P, Gaur NA, Trettin KD, Nile AH, Deminoff SJ, Dewar BJ, Wolpert M, Macdonald JM, Herman PK, Hinnebusch AG, Bankaitis VA. A sterol-binding protein integrates endosomal lipid metabolism with TOR signaling and nitrogen sensing. Cell. 2012 Feb 17;148(4):702-15. doi: 10.1016/j.cell.2011.12.026. PMID:22341443 doi:http://dx.doi.org/10.1016/j.cell.2011.12.026
↑ Im YJ, Raychaudhuri S, Prinz WA, Hurley JH. Structural mechanism for sterol sensing and transport by OSBP-related proteins. Nature. 2005 Sep 1;437(7055):154-8. PMID:16136145 doi:http://dx.doi.org/10.1038/nature03923

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 == Structural highlights ==
-The structure of the complex between Osh4 and cholesterol shows the <scene name='80/801819/Cv/2'>cholesterol binding in a tunnel</scene> covered by a lid formed by the protein N-terminal with the ligand forming numerous interactions with Osh4<ref>PMID:16136145</ref>.
+The structure of the complex between Osh4 and cholesterol shows the <scene name='80/801819/Cv/5'>cholesterol binding in a tunnel</scene> covered by a <scene name='80/801819/Cv/4'>lid formed by the protein N-terminal</scene> with the ligand forming numerous interactions with Osh4<ref>PMID:16136145</ref>.
 </StructureSection>