1opa: Difference between revisions

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OCA

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 ==THE CRYSTAL STRUCTURES OF HOLO-AND APO-CELLULAR RETINOL BINDING PROTEIN II==
-<StructureSection load='1opa' size='340' side='right' caption='[[1opa]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='1opa' size='340' side='right'caption='[[1opa]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1opa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_rat Black rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OPA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1opa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPA FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1opa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opa OCA], [http://pdbe.org/1opa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1opa RCSB], [http://www.ebi.ac.uk/pdbsum/1opa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1opa ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#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=1opa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opa OCA], [https://pdbe.org/1opa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opa RCSB], [https://www.ebi.ac.uk/pdbsum/1opa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opa ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RET2_RAT RET2_RAT]] Intracellular transport of retinol.
+[https://www.uniprot.org/uniprot/RET2_RAT RET2_RAT] Intracellular transport of retinol.
 == 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/op/1opa_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/op/1opa_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 18: / Line 19: @@
 </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=1opa ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Apo and holo-cellular retinol-binding protein II have been crystallized, and their crystal structures have been determined to 2.1 A and 1.9 A respectively. The apo and holo-crystals have different but related triclinic space groups. The X-ray phases for both structures were determined using the molecular replacement method. The crystal co-ordinates were refined to an R-factor of 0.200 for apo, and 0.173 for holo-cellular retinol-binding protein II. The holo and apo-models have nearly the same tertiary structures. Cellular retinol-binding protein II consists of a ten-stranded anti-parallel beta-barrel with the ligand binding cavity within the barrel. Two alpha-helices cover the open end of the beta-barrel making it almost solvent inaccessible. A single portal large enough to admit a water molecule was observed opening into the binding cavity. Exogenously added retinol was found within the cavity of each holo-cellular retinol-binding protein II molecule. Each retinol was surrounded by both polar and non-polar residues. The hydroxyl group of the bound retinol hydrogen bonds to the amide group of glutamine 108. The overall conformation of the bound retinol was derived from the four different molecules of holo-cellular retinol-binding protein II present in the triclinic form. The four copies of bound retinol had essentially the same conformation as found in crystalline retinaldehyde.
-Crystal structures of holo and apo-cellular retinol-binding protein II.,Winter NS, Bratt JM, Banaszak LJ J Mol Biol. 1993 Apr 20;230(4):1247-59. PMID:8487303<ref>PMID:8487303</ref>
+==See Also==
+*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1opa" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Black rat]]
+[[Category: Large Structures]]
-[[Category: Banaszak, L]]
+[[Category: Rattus rattus]]
-[[Category: Winter, N]]
+[[Category: Banaszak L]]
-[[Category: Retinol transport]]
+[[Category: Winter N]]