4j03

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'''Unreleased structure'''
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{{STRUCTURE_4j03| PDB=4j03 | SCENE= }}
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===Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant===
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{{ABSTRACT_PUBMED_23684894}}
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The entry 4j03 is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/HYES_HUMAN HYES_HUMAN]] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.<ref>PMID:12574508</ref> <ref>PMID:12574510</ref>
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Authors: Morisseau, C., Pakhomova, S., Hwang, S.H., Newcomer, M.E., Hammock, B.D.
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==About this Structure==
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[[4j03]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J03 OCA].
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Description: Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant
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==Reference==
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<ref group="xtra">PMID:023684894</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Hammock, B D.]]
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[[Category: Hwang, S H.]]
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[[Category: Morisseau, C.]]
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[[Category: Newcomer, M E.]]
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[[Category: Pakhomova, S.]]
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[[Category: Domain-swapped dimer]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]

Revision as of 08:15, 19 June 2013

Template:STRUCTURE 4j03

Contents

Crystal structure of human soluble epoxide hydrolase complexed with fulvestrant

Template:ABSTRACT PUBMED 23684894

Function

[HYES_HUMAN] Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate.[1] [2]

About this Structure

4j03 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Morisseau C, Pakhomova S, Hwang SH, Newcomer ME, Hammock BD. Inhibition of soluble epoxide hydrolase by fulvestrant and sulfoxides. Bioorg Med Chem Lett. 2013 Jul 1;23(13):3818-21. doi: 10.1016/j.bmcl.2013.04.083., Epub 2013 May 6. PMID:23684894 doi:10.1016/j.bmcl.2013.04.083
  1. ↑ Cronin A, Mowbray S, Durk H, Homburg S, Fleming I, Fisslthaler B, Oesch F, Arand M. The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1552-7. Epub 2003 Feb 6. PMID:12574508 doi:10.1073/pnas.0437829100
  2. ↑ Newman JW, Morisseau C, Harris TR, Hammock BD. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1558-63. Epub 2003 Feb 6. PMID:12574510 doi:10.1073/pnas.0437724100

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