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==Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.4 Angstrom Resolution== | ==Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.4 Angstrom Resolution== | ||
<StructureSection load='4ede' size='340' side='right' caption='[[4ede]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4ede' size='340' side='right'caption='[[4ede]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ede]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ede]] 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=4EDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDE FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
<tr id=' | <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=4ede FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ede OCA], [https://pdbe.org/4ede PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ede RCSB], [https://www.ebi.ac.uk/pdbsum/4ede PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ede ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== 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 16: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4ede" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 21: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Geiger JH]] | ||
[[Category: | [[Category: Nossoni Z]] | ||
Latest revision as of 13:47, 6 November 2024
Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.4 Angstrom ResolutionCrystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal 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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