Carnitine palmitoyltransferase
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | + | <scene name='48/485614/Cv/11'>Substrate analog interacts with CPT II</scene> ([[2rcu]]) in a <scene name='48/485614/Cv/8'>large tunnel</scene> with its <scene name='48/485614/Cv/9'>hydrophilic head group</scene> situated at the tunnel center and the <scene name='48/485614/Cv/10'>alkyl part occupying the hydrophobic part</scene> of the tunnel. <ref>PMID:17585909</ref> | |
</StructureSection> | </StructureSection> | ||
==3D structures of carnitine palmitoyltransferase== | ==3D structures of carnitine palmitoyltransferase== | ||
Revision as of 14:04, 13 February 2023
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3D structures of carnitine palmitoyltransferase
Updated on 13-February-2023
2le3 – hCPT I regulatory domain – human - NMR
2m76 - hCPT I regulatory domain – NMR
2h4t, 2fyo, 2deb – rCPT II – rat
2fw3 - rCPT II + antidiabetic drug
2rcu – rCPT II + substrate analog
4ep9, 4eph, 4eyw - rCPT II + inhibitor
References
- ↑ Bonnefont JP, Djouadi F, Prip-Buus C, Gobin S, Munnich A, Bastin J. Carnitine palmitoyltransferases 1 and 2: biochemical, molecular and medical aspects. Mol Aspects Med. 2004 Oct-Dec;25(5-6):495-520. PMID:15363638 doi:http://dx.doi.org/10.1016/j.mam.2004.06.004
- ↑ Rufer AC, Lomize A, Benz J, Chomienne O, Thoma R, Hennig M. Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog. FEBS Lett. 2007 Jul 10;581(17):3247-52. Epub 2007 Jun 8. PMID:17585909 doi:10.1016/j.febslet.2007.05.080
