2rq0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:39, 30 October 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2rq0.png|left|200px]]
 
-
{{STRUCTURE_2rq0| PDB=2rq0 | SCENE= }}
+
==Solution Structure of Mouse Lipocalin-type Prostaglandin D Synthase Possessing the Intrinsic Disulfide Bond==
 +
<StructureSection load='2rq0' size='340' side='right'caption='[[2rq0]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2rq0]] 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=2RQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RQ0 FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=2rq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rq0 OCA], [https://pdbe.org/2rq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rq0 RCSB], [https://www.ebi.ac.uk/pdbsum/2rq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rq0 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/rq/2rq0_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2rq0 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Lipocalin-type prostaglandin D synthase (L-PGDS) acts as both a PGD(2) synthase and an extracellular transporter for small lipophilic molecules. From a series of biochemical studies, it has been found that L-PGDS has an ability to bind a variety of lipophilic ligands such as biliverdin, bilirubin and retinoids in vitro. Therefore, we considered that it is necessary to clarify the molecular structure of L-PGDS upon binding ligand in order to understand the physiological relevance of L-PGDS as a transporter protein. We investigated a molecular structure of L-PGDS/biliverdin complex by small-angle X-ray scattering (SAXS) and multi-dimensional NMR measurements, and characterized the binding mechanism in detail. SAXS measurements revealed that L-PGDS has a globular shape and becomes compact by 1.3A in radius of gyration on binding biliverdin. NMR experiments revealed that L-PGDS possessed an eight-stranded antiparallel beta-barrel forming a central cavity. Upon the titration with biliverdin, some cross-peaks for residues surrounding the cavity and EF-loop and H2-helix above the beta-barrel shifted, and the intensity of other cross-peaks decreased with signal broadenings in (1)H-(15)N heteronuclear single quantum coherence spectra. These results demonstrate that L-PGDS holds biliverdin within the beta-barrel, and the conformation of the loop regions above the beta-barrel changes upon binding biliverdin. Through such a conformational change, the whole molecule of L-PGDS becomes compact.
-
===Solution Structure of Mouse Lipocalin-type Prostaglandin D Synthase Possessing the Intrinsic Disulfide Bond===
+
Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR.,Miyamoto Y, Nishimura S, Inoue K, Shimamoto S, Yoshida T, Fukuhara A, Yamada M, Urade Y, Yagi N, Ohkubo T, Inui T J Struct Biol. 2010 Feb;169(2):209-18. Epub 2009 Oct 13. PMID:19833210<ref>PMID:19833210</ref>
-
{{ABSTRACT_PUBMED_19833210}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2rq0" style="background-color:#fffaf0;"></div>
-
[[2rq0]] is a 1 chain structure of [[Prostaglandin D synthase]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQ0 OCA].
+
==See Also==
==See Also==
*[[Prostaglandin D synthase|Prostaglandin D synthase]]
*[[Prostaglandin D synthase|Prostaglandin D synthase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:019833210</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Prostaglandin-D synthase]]
+
[[Category: Inui T]]
-
[[Category: Inui, T.]]
+
[[Category: Miyamoto Y]]
-
[[Category: Miyamoto, Y.]]
+
[[Category: Nishimura S]]
-
[[Category: Nishimura, S.]]
+
-
[[Category: Beta-barrel]]
+
-
[[Category: Endoplasmic reticulum]]
+
-
[[Category: Fatty acid biosynthesis]]
+
-
[[Category: Glycoprotein]]
+
-
[[Category: Golgi apparatus]]
+
-
[[Category: Isomerase]]
+
-
[[Category: Lipid synthesis]]
+
-
[[Category: Lipocalin]]
+
-
[[Category: Membrane]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Prostaglandin biosynthesis]]
+
-
[[Category: Pyrrolidone carboxylic acid]]
+
-
[[Category: Secreted]]
+
-
[[Category: Transport]]
+

Current revision

Solution Structure of Mouse Lipocalin-type Prostaglandin D Synthase Possessing the Intrinsic Disulfide Bond

PDB ID 2rq0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rq0"
Personal tools