4yfq: Difference between revisions
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</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> | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ybp|4ybp]], [[4ybu|4ybu]], [[4i9s|4i9s]], [[2g7b|2g7b]], [[4ruu|4ruu]], [[4eej|4eej]], [[4yfp|4yfp]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ybp|4ybp]], [[4ybu|4ybu]], [[4i9s|4i9s]], [[2g7b|2g7b]], [[4ruu|4ruu]], [[4eej|4eej]], [[4yfp|4yfp]]</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=4yfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yfq OCA], [http://pdbe.org/4yfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yfq RCSB], [http://www.ebi.ac.uk/pdbsum/4yfq PDBsum]</span></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=4yfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yfq OCA], [http://pdbe.org/4yfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yfq RCSB], [http://www.ebi.ac.uk/pdbsum/4yfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yfq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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. | [[http://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;"> | |||
== Publication Abstract from PubMed == | |||
The members of the rhodopsin family of proteins are involved in many essential light-dependent processes in biology. Specific photoisomerization of the protein-bound retinylidene PSB at a specified wavelength range of light is at the heart of all of these systems. Nonetheless, it has been difficult to reproduce in an engineered system. We have developed rhodopsin mimics, using intracellular lipid binding protein family members as scaffolds, to study fundamental aspects of protein/chromophore interactions. Herein we describe a system that specifically isomerizes the retinylidene protonated Schiff base both thermally and photochemically. This isomerization has been characterized at atomic resolution by quantitatively interconverting the isomers in the crystal both thermally and photochemically. This event is accompanied by a large pKa change of the imine similar to the pKa changes observed in bacteriorhodopsin and visual opsins during isomerization. | |||
A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.,Nosrati M, Berbasova T, Vasileiou C, Borhan B, Geiger JH J Am Chem Soc. 2016 Jul 5. PMID:27310917<ref>PMID:27310917</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4yfq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 20:45, 12 July 2016
CRYSTAL STRUCTURE OF THE R111K:Y134F:T54V:R132Q:P39Y:R59Y MUTANT OF HUMAN CELLULAR RETINOIC ACID BINDING PROTEINII WITH RETINAL AFTER 24 HOURS INCUBATION AT 1.62 ANGSTROM RESOLUTION - Thermodynamic product - 1st cycleCRYSTAL STRUCTURE OF THE R111K:Y134F:T54V:R132Q:P39Y:R59Y MUTANT OF HUMAN CELLULAR RETINOIC ACID BINDING PROTEINII WITH RETINAL AFTER 24 HOURS INCUBATION AT 1.62 ANGSTROM RESOLUTION - Thermodynamic product - 1st cycle
Structural highlights
Function[RABP2_HUMAN] Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors. Publication Abstract from PubMedThe members of the rhodopsin family of proteins are involved in many essential light-dependent processes in biology. Specific photoisomerization of the protein-bound retinylidene PSB at a specified wavelength range of light is at the heart of all of these systems. Nonetheless, it has been difficult to reproduce in an engineered system. We have developed rhodopsin mimics, using intracellular lipid binding protein family members as scaffolds, to study fundamental aspects of protein/chromophore interactions. Herein we describe a system that specifically isomerizes the retinylidene protonated Schiff base both thermally and photochemically. This isomerization has been characterized at atomic resolution by quantitatively interconverting the isomers in the crystal both thermally and photochemically. This event is accompanied by a large pKa change of the imine similar to the pKa changes observed in bacteriorhodopsin and visual opsins during isomerization. A Photoisomerizing Rhodopsin Mimic Observed at Atomic Resolution.,Nosrati M, Berbasova T, Vasileiou C, Borhan B, Geiger JH J Am Chem Soc. 2016 Jul 5. PMID:27310917[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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