2fr3: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2fr3.gif|left|200px]]<br />
-<applet load="2fr3" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2fr3, resolution 1.48&Aring;" />
-'''Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 Angstroms Resolution'''<br />
-==Overview==
+==Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with All-Trans-Retinoic Acid at 1.48 Angstroms Resolution==
-CRABPII is a small, cytosolic protein that solubilizes and transfers, retinoic acid (RA) to the nucleus while also enhancing its transcriptional, activity. We have determined the first high-resolution structure of, apo-wild type (WT) CRABPII at 1.35 A. Using three different data sets, collected on apo-WT CRABPII we have shown that apo- and holo-CRABPII share, very similar structures. Binding of RA appears to increase the overall, rigidity of the structure, although the induced structural changes are not, as pronounced as previously thought. The enhanced structural rigidity may, be an important determinant for the enhanced nuclear localization of the, RA-bound protein. Comparison of our apo-WT with a mutant apo-CRABPII, structure shows that mutation of Arg111, a conserved residue of CRABPII, and a key residue in RA binding, causes structural changes in the, molecule. We further investigated the structural importance of conserved, residues by determining the structure of the F15W mutant CRABPII, (F15W-CRABPII). Our structures also demonstrate structural changes induced, by crystal packing and show that a crystal can harbor demonstrative, structural differences in the asymmetric unit.
+<StructureSection load='2fr3' size='340' side='right'caption='[[2fr3]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2fr3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FR3 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene></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=2fr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fr3 OCA], [https://pdbe.org/2fr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fr3 RCSB], [https://www.ebi.ac.uk/pdbsum/2fr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fr3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RABP2_HUMAN RABP2_HUMAN] Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.
+== 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/fr/2fr3_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=2fr3 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACT and REA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FR3 OCA].
+*[[CRABP I ( Cellular Retinoic Acid Binding Protein )|CRABP I ( Cellular Retinoic Acid Binding Protein )]]
+*[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]]
-==Reference==
+*[[Gustavo Elberto Epalza Sanchez/Sandbox 1|Gustavo Elberto Epalza Sanchez/Sandbox 1]]
-The structure of Apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation., Vaezeslami S, Mathes E, Vasileiou C, Borhan B, Geiger JH, J Mol Biol. 2006 Oct 27;363(3):687-701. Epub 2006 Aug 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16979656 16979656]
+*[[Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)|Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)]]
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Geiger, J.H.]]
+[[Category: Geiger JH]]
-[[Category: Vaezeslami, S.]]
+[[Category: Vaezeslami S]]
-[[Category: ACT]]
-[[Category: REA]]
-[[Category: beta barrel]]
-[[Category: crabpii]]
-[[Category: crystallography]]
-[[Category: high resolution]]
-[[Category: retinoic acid]]
-[[Category: retinoids]]
-[[Category: x-ray]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:09:24 2007''