Fatty acid synthase

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== Relevance ==
== Relevance ==
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FAS is as target of anti-cancer drugs. FAS from Mycobacterium tuberculosis inhibitors are possible anti-tuberculosis drugs<ref>PMID:30150274</ref> .
+
FAS is as target of anti-cancer drugs. FAS from Mycobacterium tuberculosis inhibitors are possible anti-tuberculosis drugs<ref>PMID:30250274</ref> .
== Structural insights ==
== Structural insights ==

Revision as of 08:05, 27 June 2019

Human FAS thioesterase domain complex with fatty acid (PDB code 3tjm)

Drag the structure with the mouse to rotate

References

  1. Smith S, Witkowski A, Joshi AK. Structural and functional organization of the animal fatty acid synthase. Prog Lipid Res. 2003 Jul;42(4):289-317. PMID:12689621
  2. Elad N, Baron S, Peleg Y, Albeck S, Grunwald J, Raviv G, Shakked Z, Zimhony O, Diskin R. Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 A resolution. Nat Commun. 2018 Sep 24;9(1):3886. doi: 10.1038/s41467-018-06440-6. PMID:30250274 doi:http://dx.doi.org/10.1038/s41467-018-06440-6
  3. Zhang W, Chakravarty B, Zheng F, Gu Z, Wu H, Mao J, Wakil SJ, Quiocho FA. Crystal structure of FAS thioesterase domain with polyunsaturated fatty acyl adduct and inhibition by dihomo-{gamma}-linolenic acid. Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15757-62. Epub 2011 Sep 9. PMID:21908709 doi:10.1073/pnas.1112334108

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