Leukotriene B4 hydroxydehydrogenase

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== Structural highlights ==
== Structural highlights ==
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<scene name='43/433641/Cv/4'>LB4H active site is located at the hydrophobic pore</scene> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}) on the dimer interface<ref>PMID:15007077</ref>. <scene name='43/433641/Cv/6'>Pore</scene>.
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<scene name='43/433641/Cv/7'>LB4H active site is located at the hydrophobic pore</scene> ({{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}) on the dimer interface<ref>PMID:15007077</ref>. <scene name='43/433641/Cv/8'>Pore</scene>.
</StructureSection>
</StructureSection>
== Structural highlights ==
== Structural highlights ==

Revision as of 09:38, 7 July 2019

Guinea pig leukotriene B4 hydroxydehydrogenase complex with oxo-PGE2, NADP an Cl- ion (green)(PDB entry 1v3v)

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Structural highlights

3D Structures of Leukotriene B4 hydroxydehydrogenase

1zsv – LB4H - human
2dm6 –gpLB4H/15-oxo-prostaglandin 13-reductase+indomethacin – guinea pig
1v3t, 1v3u - gpLB4H/15-oxo-prostaglandin 13-reductase
1v3v - gpLB4H/15-oxo-prostaglandin 13-reductase+NADP+15-oxo-PGE-2

References

  1. ↑ Tobin DM, Roca FJ, Ray JP, Ko DC, Ramakrishnan L. An enzyme that inactivates the inflammatory mediator leukotriene b4 restricts mycobacterial infection. PLoS One. 2013 Jul 11;8(7):e67828. doi: 10.1371/journal.pone.0067828. Print 2013. PMID:23874453 doi:http://dx.doi.org/10.1371/journal.pone.0067828
  2. ↑ Hori T, Yokomizo T, Ago H, Sugahara M, Ueno G, Yamamoto M, Kumasaka T, Shimizu T, Miyano M. Structural basis of leukotriene B4 12-hydroxydehydrogenase/15-Oxo-prostaglandin 13-reductase catalytic mechanism and a possible Src homology 3 domain binding loop. J Biol Chem. 2004 May 21;279(21):22615-23. Epub 2004 Mar 8. PMID:15007077 doi:10.1074/jbc.M312655200

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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