1utg: Difference between revisions

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-{{Seed}}
-[[Image:1utg.png|left|200px]]
-<!--
+==REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION==
-The line below this paragraph, containing "STRUCTURE_1utg", creates the "Structure Box" on the page.
+<StructureSection load='1utg' size='340' side='right'caption='[[1utg]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1utg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UTG FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.34&#8491;</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=1utg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1utg OCA], [https://pdbe.org/1utg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1utg RCSB], [https://www.ebi.ac.uk/pdbsum/1utg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1utg ProSAT]</span></td></tr>
-{{STRUCTURE_1utg|  PDB=1utg  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/UTER_RABIT UTER_RABIT] Uteroglobin binds progesterone specifically and with high affinity. It may regulate progesterone concentrations reaching the blastocyst. It is also a potent inhibitor of phospholipase A2.
+== 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/ut/1utg_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=1utg ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The structure of uteroglobin, a progesterone binding protein from rabbit uterine fluid, was determined and refined at 1.34 A resolution to a conventional R-factor of 0.229. The accuracy of the co-ordinates is estimated to be 0.15 A. The isotropic temperature factor of individual atoms was refined and its average value is 11.9 A2 for the 548 non-hydrogen atoms of the protein monomer. A total of 83 water molecules was located in difference electron density maps and refined, first using a constant occupancy factor of 1 and then variable occupancy, the final (Q) being 0.63. The mean temperature factor of the water oxygen atoms is 26.4 A2. Uteroglobin is a dimer and its secondary structure consists of four alpha-helices per monomer that align in an anti-parallel fashion. There is one beta-turn between helix 2 and helix 3 (Lys26 to Glu29); 76% of the residues are part of the alpha-helices. In the core of the dimeric protein molecule, between the two monomers that are held together by two disulfide bridges, we have observed a closed cavity. Its length is 15.6 A and its width is 9 A; 14 water molecules could be positioned inside. In the "bottom" part of the protein, near the C terminus, we have observed a smaller cavity, occupied by two water molecules. The calculation of the molecular surface revealed four surface pockets whose possible functional implications are discussed below.
-===REFINEMENT OF THE C2221 CRYSTAL FORM OF OXIDIZED UTEROGLOBIN AT 1.34 ANGSTROMS RESOLUTION===
+Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution.,Morize I, Surcouf E, Vaney MC, Epelboin Y, Buehner M, Fridlansky F, Milgrom E, Mornon JP J Mol Biol. 1987 Apr 20;194(4):725-39. PMID:3656405<ref>PMID:3656405</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_3656405}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1utg" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 3656405 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_3656405}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-UTG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UTG OCA].
-==Reference==
-Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution., Morize I, Surcouf E, Vaney MC, Epelboin Y, Buehner M, Fridlansky F, Milgrom E, Mornon JP, J Mol Biol. 1987 Apr 20;194(4):725-39. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3656405 3656405]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Buehner M]]
-[[Category: Buehner, M.]]
+[[Category: Morize I]]
-[[Category: Morize, I.]]
+[[Category: Mornon JP]]
-[[Category: Mornon, J P.]]
+[[Category: Surcouf E]]
-[[Category: Surcouf, E.]]
+[[Category: Vaney MC]]
-[[Category: Vaney, M C.]]
-[[Category: Steroid binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:57:00 2008''