3vhh: Difference between revisions
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The | ==Crystal structure of DiMe-biotin-avidin complex== | ||
<StructureSection load='3vhh' size='340' side='right'caption='[[3vhh]], [[Resolution|resolution]] 2.26Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vhh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VHH 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]] 2.26Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VHH:5-[(3AS,4S,6AR)-1,3-DIMETHYL-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANOIC+ACID'>VHH</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=3vhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vhh OCA], [https://pdbe.org/3vhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vhh RCSB], [https://www.ebi.ac.uk/pdbsum/3vhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vhh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AVID_CHICK AVID_CHICK] The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Biotin-(strept)avidin complex is widely used in biotechnology because of its extremely high binding constant, but there is no report describing spatiotemporally controlled formation of the complex in live cells. Here, based on X-ray crystal structure analysis and calorimetric data, we designed and synthesized photoreleasable biotins, which show greatly reduced affinity for (strept)avidin, but recover native affinity after UV irradiation. For application at the cell surface, we introduced an amine-reactive moiety into these "caged" biotin molecules. Specific fluorescence imaging of live cells that had been labeled with these agents and then UV-irradiated, was accomplished by addition of streptavidin conjugated with a fluorophore. We also demonstrated the applicability of these compounds for UV-irradiated-cell-specific drug delivery by using caged-biotin-labeled cells, a prodrug, and streptavidin conjugated with a prodrug-activating enzyme. | |||
Rational development of caged-biotin protein-labeling agents and some applications in live cells.,Terai T, Maki E, Sugiyama S, Takahashi Y, Matsumura H, Mori Y, Nagano T Chem Biol. 2011 Oct 28;18(10):1261-72. PMID:22035795<ref>PMID:22035795</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vhh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Avidin 3D structures|Avidin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | |||
[[Category: Maki E]] | |||
[[Category: Matsumura H]] | |||
[[Category: Mori Y]] | |||
[[Category: Nagano T]] | |||
[[Category: Sugiyama S]] | |||
[[Category: Takahashi Y]] | |||
[[Category: Terai T]] | |||
Latest revision as of 15:22, 8 November 2023
Crystal structure of DiMe-biotin-avidin complexCrystal structure of DiMe-biotin-avidin complex
Structural highlights
FunctionAVID_CHICK The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin). Publication Abstract from PubMedBiotin-(strept)avidin complex is widely used in biotechnology because of its extremely high binding constant, but there is no report describing spatiotemporally controlled formation of the complex in live cells. Here, based on X-ray crystal structure analysis and calorimetric data, we designed and synthesized photoreleasable biotins, which show greatly reduced affinity for (strept)avidin, but recover native affinity after UV irradiation. For application at the cell surface, we introduced an amine-reactive moiety into these "caged" biotin molecules. Specific fluorescence imaging of live cells that had been labeled with these agents and then UV-irradiated, was accomplished by addition of streptavidin conjugated with a fluorophore. We also demonstrated the applicability of these compounds for UV-irradiated-cell-specific drug delivery by using caged-biotin-labeled cells, a prodrug, and streptavidin conjugated with a prodrug-activating enzyme. Rational development of caged-biotin protein-labeling agents and some applications in live cells.,Terai T, Maki E, Sugiyama S, Takahashi Y, Matsumura H, Mori Y, Nagano T Chem Biol. 2011 Oct 28;18(10):1261-72. PMID:22035795[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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