2e4j: Difference between revisions

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New page: left|200px<br /><applet load="2e4j" size="450" color="white" frame="true" align="right" spinBox="true" caption="2e4j" /> '''Solution Structure of mouse Lipocalin-type P...
 
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[[Image:2e4j.jpg|left|200px]]<br /><applet load="2e4j" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2e4j" />
'''Solution Structure of mouse Lipocalin-type Prostaglandin D Synthase'''<br />


==About this Structure==
==Solution Structure of mouse Lipocalin-type Prostaglandin D Synthase==
2E4J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Active as [http://en.wikipedia.org/wiki/Prostaglandin-D_synthase Prostaglandin-D synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.99.2 5.3.99.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2E4J OCA].  
<StructureSection load='2e4j' size='340' side='right'caption='[[2e4j]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2e4j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E4J FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e4j OCA], [https://pdbe.org/2e4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e4j RCSB], [https://www.ebi.ac.uk/pdbsum/2e4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e4j ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTGDS_MOUSE PTGDS_MOUSE] Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system.<ref>PMID:8922532</ref> <ref>PMID:9892701</ref> <ref>PMID:10781097</ref> <ref>PMID:11751991</ref> <ref>PMID:12077186</ref> <ref>PMID:17715133</ref> <ref>PMID:19546224</ref> <ref>PMID:19833210</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/2e4j_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2e4j ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Prostaglandin D synthase|Prostaglandin D synthase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Prostaglandin-D synthase]]
[[Category: Ohkubo T]]
[[Category: Single protein]]
[[Category: Shimamoto S]]
[[Category: Ohkubo, T.]]
[[Category: Shimamoto, S.]]
[[Category: isomerase]]
[[Category: pgds]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:56:25 2007''

Latest revision as of 21:47, 29 May 2024

Solution Structure of mouse Lipocalin-type Prostaglandin D SynthaseSolution Structure of mouse Lipocalin-type Prostaglandin D Synthase

Structural highlights

2e4j is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTGDS_MOUSE Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system.[1] [2] [3] [4] [5] [6] [7] [8]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Hoffmann A, Bachner D, Betat N, Lauber J, Gross G. Developmental expression of murine Beta-trace in embryos and adult animals suggests a function in maturation and maintenance of blood-tissue barriers. Dev Dyn. 1996 Nov;207(3):332-43. PMID:8922532 doi:<332::AID-AJA10>3.0.CO;2-6 http://dx.doi.org/10.1002/(SICI)1097-0177(199611)207:3<332::AID-AJA10>3.0.CO;2-6
  2. ↑ Eguchi N, Minami T, Shirafuji N, Kanaoka Y, Tanaka T, Nagata A, Yoshida N, Urade Y, Ito S, Hayaishi O. Lack of tactile pain (allodynia) in lipocalin-type prostaglandin D synthase-deficient mice. Proc Natl Acad Sci U S A. 1999 Jan 19;96(2):726-30. PMID:9892701
  3. ↑ Pinzar E, Kanaoka Y, Inui T, Eguchi N, Urade Y, Hayaishi O. Prostaglandin D synthase gene is involved in the regulation of non-rapid eye movement sleep. Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4903-7. PMID:10781097 doi:http://dx.doi.org/10.1073/pnas.090093997
  4. ↑ Fujitani Y, Kanaoka Y, Aritake K, Uodome N, Okazaki-Hatake K, Urade Y. Pronounced eosinophilic lung inflammation and Th2 cytokine release in human lipocalin-type prostaglandin D synthase transgenic mice. J Immunol. 2002 Jan 1;168(1):443-9. PMID:11751991
  5. ↑ Taniike M, Mohri I, Eguchi N, Beuckmann CT, Suzuki K, Urade Y. Perineuronal oligodendrocytes protect against neuronal apoptosis through the production of lipocalin-type prostaglandin D synthase in a genetic demyelinating model. J Neurosci. 2002 Jun 15;22(12):4885-96. PMID:12077186
  6. ↑ Shimamoto S, Yoshida T, Inui T, Gohda K, Kobayashi Y, Fujimori K, Tsurumura T, Aritake K, Urade Y, Ohkubo T. NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity. J Biol Chem. 2007 Oct 26;282(43):31373-9. Epub 2007 Aug 22. PMID:17715133 doi:10.1074/jbc.M700123200
  7. ↑ Kumasaka T, Aritake K, Ago H, Irikura D, Tsurumura T, Yamamoto M, Miyano M, Urade Y, Hayaishi O. Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase. J Biol Chem. 2009 Aug 14;284(33):22344-52. Epub 2009 Jun 22. PMID:19546224 doi:10.1074/jbc.M109.018341
  8. ↑ Miyamoto Y, Nishimura S, Inoue K, Shimamoto S, Yoshida T, Fukuhara A, Yamada M, Urade Y, Yagi N, Ohkubo T, Inui T. Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR. J Struct Biol. 2010 Feb;169(2):209-18. Epub 2009 Oct 13. PMID:19833210 doi:10.1016/j.jsb.2009.10.005
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