5f9x: Difference between revisions

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-'''Unreleased structure'''
-The entry 5f9x is ON HOLD  until Paper Publication
+==X-RAY STRUCTURE OF THE ADDUCT BETWEEN HEN EGG WHITE LYSOZYME AND CISPLATIN UPON 24 HOURS OF INCUBATION AT 55 DEGREES==
+<StructureSection load='5f9x' size='340' side='right'caption='[[5f9x]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5f9x]] 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=5F9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F9X 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]] 1.94&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPT:CISPLATIN'>CPT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5f9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f9x OCA], [https://pdbe.org/5f9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f9x RCSB], [https://www.ebi.ac.uk/pdbsum/5f9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f9x 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 ==
+The products of the reaction between cisplatin (CDDP) and the model protein hen egg white lysozyme (HEWL) at 20, 37 and 55 degrees C in pure water were studied by UV-Vis absorption spectroscopy, intrinsic fluorescence and circular dichroism, dynamic and electrophoretic light scattering and inductively coupled plasma mass spectrometry. X-ray structures were also solved for the adducts formed at 20 and 55 degrees C. Data demonstrate that high temperature facilitates the formation of CDDP-HEWL adducts, where Pt atoms bind ND1 atom of His15 or NE2 atom of His15 and NH1 atom of Arg14. Our study suggests that high human body temperature (fever) could increase the rate of drug binding to proteins thus enhancing possible toxic side effects related to CDDP administration.
-Authors: Russo Krauss, I., Ferraro, G., Pica, A., Merlino, A.
+Effect of temperature on the interaction of cisplatin with the model protein hen egg white lysozyme.,Ferraro G, Pica A, Russo Krauss I, Pane F, Amoresano A, Merlino A J Biol Inorg Chem. 2016 Apr 4. PMID:27040953<ref>PMID:27040953</ref>
-Description: X-RAY STRUCTURE OF THE ADDUCT BETWEEN HEN EGG WHITE LYSOZYME AND CISPLATIN UPON 24 HOURS OF INCUBATION AT 55 DEGREES
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Ferraro, G]]
+<div class="pdbe-citations 5f9x" style="background-color:#fffaf0;"></div>
-[[Category: Merlino, A]]
-[[Category: Russo Krauss, I]]
+==See Also==
-[[Category: Pica, A]]
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Gallus gallus]]
+[[Category: Large Structures]]
+[[Category: Ferraro G]]
+[[Category: Merlino A]]
+[[Category: Pica A]]
+[[Category: Russo Krauss I]]