View source for 29ol


==X-ray structure of the adduct formed upon reaction of the gold compound AF-Npx with lysozyme (Structure 2)==
<StructureSection load='29ol' size='340' side='right'caption='[[29ol]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[29ol]] is a 1 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=29OL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=29OL 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]] 1.441&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</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=29ol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=29ol OCA], [https://pdbe.org/29ol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=29ol RCSB], [https://www.ebi.ac.uk/pdbsum/29ol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=29ol ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_CHICK LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.<ref>PMID:22044478</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Au(I) complexes are widely investigated as therapeutic agents due to their high affinity for biological nucleophiles and protein targets. Here, the reactivity of an Auranofin (AF) derivative bearing naproxen as a ligand toward hen egg white lysozyme (HEWL) was investigated by a combined crystallographic and computational approach. Notably, the first observation of lysine metalation in HEWL by an Au complex is reported. The results highlight how ligand substitution can significantly affect Au(I) reactivity toward biomacromolecules, enabling noncanonical targeting and potentially impacting biological activity.

Tuning Au Reactivity Beyond Canonical Targets: Ligand-Driven Au(I) Metalation of Lysine Residues in Hen Egg White Lysozyme.,Piroddu D, Famlonga L, Tolbatov I, Ferraro G, Chiaverini L, Merlino A, La Mendola D, Marrone A, Marzo T Inorg Chem. 2026 Jul 20;65(28):16296-16304. doi: 10.1021/acs.inorgchem.6c01884. , Epub 2026 Jul 8. PMID:42417613<ref>PMID:42417613</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 29ol" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Ferraro G]]
[[Category: Merlino A]]