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==Crystal structure of the Q108K:K40L mutant of human Cellular Retinol Binding ProteinII in complex with All-trans-Retinal after 24 hour incubation at 1.4 Angstrom Resolution== | ==Crystal structure of the Q108K:K40L mutant of human Cellular Retinol Binding ProteinII in complex with All-trans-Retinal after 24 hour incubation at 1.4 Angstrom Resolution== | ||
<StructureSection load='4ruu' size='340' side='right' caption='[[4ruu]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4ruu' size='340' side='right'caption='[[4ruu]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ruu]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ruu]] is a 2 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=4RUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RUU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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=ACT:ACETATE+ION'>ACT</scene>, <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=4ruu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ruu OCA], [https://pdbe.org/4ruu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ruu RCSB], [https://www.ebi.ac.uk/pdbsum/4ruu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ruu 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/RET2_HUMAN RET2_HUMAN] Intracellular transport of retinol. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 4ruu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ruu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Geiger JH]] | ||
[[Category: | [[Category: Nosrati M]] | ||
Revision as of 11:29, 8 March 2023
Crystal structure of the Q108K:K40L mutant of human Cellular Retinol Binding ProteinII in complex with All-trans-Retinal after 24 hour incubation at 1.4 Angstrom ResolutionCrystal structure of the Q108K:K40L mutant of human Cellular Retinol Binding ProteinII in complex with All-trans-Retinal after 24 hour incubation at 1.4 Angstrom Resolution
Structural highlights
FunctionRET2_HUMAN Intracellular transport of retinol. Publication Abstract from PubMedProtein-chromophore interactions are a central component of a wide variety of critical biological processes such as color vision and photosynthesis. To understand the fundamental elements that contribute to spectral tuning of a chromophore inside the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully encapsulate all-trans-retinal and form a covalent bond as a protonated Schiff base. This system, using rational mutagenesis designed to alter the electrostatic environment within the binding pocket of the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to 644 nanometers. With only nine point mutations, the hCRBPII mutants induced a systematic shift in the absorption profile of all-trans-retinal of more than 200 nanometers across the visible spectrum. Tuning the electronic absorption of protein-embedded all-trans-retinal.,Wang W, Nossoni Z, Berbasova T, Watson CT, Yapici I, Lee KS, Vasileiou C, Geiger JH, Borhan B Science. 2012 Dec 7;338(6112):1340-3. doi: 10.1126/science.1226135. PMID:23224553[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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