6zsr: Difference between revisions
New page: '''Unreleased structure''' The entry 6zsr is ON HOLD Authors: Balasco, N., Ferraro, G., Merlino, A. Description: Crystal structure of the Cisplatin beta-Lactoglobulin adduct formed aft... |
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==Crystal structure of the Cisplatin beta-Lactoglobulin adduct formed after 72 h of soaking== | |||
<StructureSection load='6zsr' size='340' side='right'caption='[[6zsr]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZSR 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]] 2.005Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH3:AMMONIA'>NH3</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6zsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zsr OCA], [https://pdbe.org/6zsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zsr RCSB], [https://www.ebi.ac.uk/pdbsum/6zsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zsr ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-Lactoglobulin is a major globular milk whey carrier with potential applications as an oral drug delivery system. Herein, the interactions between beta-lactoglobulin and cisplatin are investigated by UV-Vis absorption spectroscopy, circular dichroism, X-ray crystallography and electrospray ionization mass spectrometry. Structural data indicate that the protein retains its conformation upon cisplatin binding. Pt-containing fragments bind the side chains of Met7, His146 and Lys8, with the number of binding sites increasing over time. Mass spectrometry data indicate that [Pt(NH3)2Cl+], [Pt(NH3)2OH22+] and [Pt(NH3)22+] fragments interact with beta-lactoglobulin; up to 3 cisplatin fragments can bind the protein and the number of cisplatin binding sites increases over time. This work opens a new pathway in pharmaceutical studies based on a rational design of metal-based drug/beta-lactoglobulin adducts as delivering vehicles of metallodrugs. | |||
Cisplatin binding to beta-lactoglobulin: a structural study.,Balasco N, Ferraro G, Loreto D, Iacobucci I, Monti M, Merlino A Dalton Trans. 2020 Sep 15;49(35):12450-12457. doi: 10.1039/d0dt02582h. PMID:32852026<ref>PMID:32852026</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Balasco | <div class="pdbe-citations 6zsr" style="background-color:#fffaf0;"></div> | ||
[[Category: Ferraro | |||
[[Category: Merlino | ==See Also== | ||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Balasco N]] | |||
[[Category: Ferraro G]] | |||
[[Category: Merlino A]] | |||
Latest revision as of 16:22, 6 November 2024
Crystal structure of the Cisplatin beta-Lactoglobulin adduct formed after 72 h of soakingCrystal structure of the Cisplatin beta-Lactoglobulin adduct formed after 72 h of soaking
Structural highlights
Publication Abstract from PubMedbeta-Lactoglobulin is a major globular milk whey carrier with potential applications as an oral drug delivery system. Herein, the interactions between beta-lactoglobulin and cisplatin are investigated by UV-Vis absorption spectroscopy, circular dichroism, X-ray crystallography and electrospray ionization mass spectrometry. Structural data indicate that the protein retains its conformation upon cisplatin binding. Pt-containing fragments bind the side chains of Met7, His146 and Lys8, with the number of binding sites increasing over time. Mass spectrometry data indicate that [Pt(NH3)2Cl+], [Pt(NH3)2OH22+] and [Pt(NH3)22+] fragments interact with beta-lactoglobulin; up to 3 cisplatin fragments can bind the protein and the number of cisplatin binding sites increases over time. This work opens a new pathway in pharmaceutical studies based on a rational design of metal-based drug/beta-lactoglobulin adducts as delivering vehicles of metallodrugs. Cisplatin binding to beta-lactoglobulin: a structural study.,Balasco N, Ferraro G, Loreto D, Iacobucci I, Monti M, Merlino A Dalton Trans. 2020 Sep 15;49(35):12450-12457. doi: 10.1039/d0dt02582h. PMID:32852026[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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