8d6l
From Proteopedia
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<table><tr><td colspan='2'>[[8d6l]] 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=8D6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D6L FirstGlance]. <br> | <table><tr><td colspan='2'>[[8d6l]] 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=8D6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D6L 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]] 1.69Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</td></tr> | ||
| - | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RH6:( | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=RH6:7-(diethylamino)-3-[(1E)-prop-1-en-1-yl]-2H-1-benzopyran-2-one'>RH6</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=8d6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d6l OCA], [https://pdbe.org/8d6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d6l RCSB], [https://www.ebi.ac.uk/pdbsum/8d6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d6l ProSAT]</span></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=8d6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d6l OCA], [https://pdbe.org/8d6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d6l RCSB], [https://www.ebi.ac.uk/pdbsum/8d6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d6l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Cysteine-based Michael addition is a widely employed strategy for covalent conjugation of proteins, peptides, and drugs. The covalent reaction is irreversible in most cases, leading to a lack of control over the process. Utilizing spectroscopic analyses along with X-ray crystallographic studies, we demonstrate Michael addition of an engineered cysteine residue in human Cellular Retinol Binding Protein II (hCRBPII) with a coumarin analog that creates a non-fluorescent complex. UV-illumination reverses the conjugation, yielding a fluorescent species, presumably through a retro-Michael process. This series of events can be repeated between a bound and non-bound form of the cysteine reversibly, resulting in the ON-OFF control of fluorescence. The details of the mechanism of photoswitching was illuminated by recapitulation of the process in light irradiated single crystals, confirming the mechanism at atomic resolution. | Cysteine-based Michael addition is a widely employed strategy for covalent conjugation of proteins, peptides, and drugs. The covalent reaction is irreversible in most cases, leading to a lack of control over the process. Utilizing spectroscopic analyses along with X-ray crystallographic studies, we demonstrate Michael addition of an engineered cysteine residue in human Cellular Retinol Binding Protein II (hCRBPII) with a coumarin analog that creates a non-fluorescent complex. UV-illumination reverses the conjugation, yielding a fluorescent species, presumably through a retro-Michael process. This series of events can be repeated between a bound and non-bound form of the cysteine reversibly, resulting in the ON-OFF control of fluorescence. The details of the mechanism of photoswitching was illuminated by recapitulation of the process in light irradiated single crystals, confirming the mechanism at atomic resolution. | ||
| - | Light controlled reversible Michael addition of cysteine: a new tool for dynamic site-specific labeling of proteins.,Maity S, Bingham C, Sheng W, Ehyaei N, Chakraborty D, Tahmasebi-Nick S, Kimmel TE, Vasileiou C, Geiger JH, Borhan B Analyst. 2023 | + | Light controlled reversible Michael addition of cysteine: a new tool for dynamic site-specific labeling of proteins.,Maity S, Bingham C, Sheng W, Ehyaei N, Chakraborty D, Tahmasebi-Nick S, Kimmel TE, Vasileiou C, Geiger JH, Borhan B Analyst. 2023 Feb 27;148(5):1085-1092. doi: 10.1039/d2an01395a. PMID:36722993<ref>PMID:36722993</ref> |
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> | ||
Current revision
Q108K:K40L:T51C:T53A:R58L:Q38F:Q4F mutant of hCRBPII bound to synthetic fluorophore CM1V
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