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==Crystal structure of the R111K:R132Q:Y134F:T54V:R59W:A32W mutant of the Cellular Retinoic Acid Binding Protein Type II in complex with All-Trans Retinal at 2.57 Angstrom Resolution== | ==Crystal structure of the R111K:R132Q:Y134F:T54V:R59W:A32W mutant of the Cellular Retinoic Acid Binding Protein Type II in complex with All-Trans Retinal at 2.57 Angstrom Resolution== | ||
<StructureSection load='4m7m' size='340' side='right' caption='[[4m7m]], [[Resolution|resolution]] 2.57Å' scene=''> | <StructureSection load='4m7m' size='340' side='right'caption='[[4m7m]], [[Resolution|resolution]] 2.57Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4m7m]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4m7m]] 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=4M7M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M7M FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RET:RETINAL'>RET</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=4m7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m7m OCA], [https://pdbe.org/4m7m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m7m RCSB], [https://www.ebi.ac.uk/pdbsum/4m7m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m7m ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == 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. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Cellular retinoic acid-binding protein|Cellular retinoic acid-binding protein]] | *[[Cellular retinoic acid-binding protein 3D structures|Cellular retinoic acid-binding protein 3D structures]] | ||
*[[Gustavo Elberto Epalza Sanchez/Sandbox 1|Gustavo Elberto Epalza Sanchez/Sandbox 1]] | *[[Gustavo Elberto Epalza Sanchez/Sandbox 1|Gustavo Elberto Epalza Sanchez/Sandbox 1]] | ||
== References == | == References == | ||
| Line 28: | Line 26: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Geiger JH]] | ||
[[Category: | [[Category: Nosrati M]] | ||
Revision as of 14:01, 21 December 2022
Crystal structure of the R111K:R132Q:Y134F:T54V:R59W:A32W mutant of the Cellular Retinoic Acid Binding Protein Type II in complex with All-Trans Retinal at 2.57 Angstrom ResolutionCrystal structure of the R111K:R132Q:Y134F:T54V:R59W:A32W mutant of the Cellular Retinoic Acid Binding Protein Type II in complex with All-Trans Retinal at 2.57 Angstrom Resolution
Structural highlights
FunctionRABP2_HUMAN Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Publication Abstract from PubMedReengineering of Cellular Retinoic Acid Binding Protein II (CRABPII) to be capable of binding retinal as a protonated Schiff base is described. Through rational alterations of the binding pocket, electrostatic perturbations of the embedded retinylidene chromophore that favor charge delocalization of the iminium charge lead to exquisite control in the regulation of chromophoric absorption properties, spanning the visible spectrum (474-640 nm). The pKa of the retinylidine protonated Schiff base was modulated from 2.4 to 8.1, giving rise to a set of proteins of varying colors and pH sensitivities. These proteins were used to demonstrate a concentration independent, ratiometric pH sensor. Rational Design of a Colorimetric pH Sensor from a Soluble Retinoic Acid Chaperone.,Berbasova T, Nosrati M, Vasileiou C, Wang W, Lee KS, Yapici I, Geiger JH, Borhan B J Am Chem Soc. 2013 Sep 20. PMID:24059243[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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