4ppo: Difference between revisions

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New page: '''Unreleased structure''' The entry 4ppo is ON HOLD Authors: Messori, L., Merlino, A: Description: First Crystal Structure for an Oxaliplatin-Protein Complex
 
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'''Unreleased structure'''


The entry 4ppo is ON HOLD
==First Crystal Structure for an Oxaliplatin-Protein Complex==
<StructureSection load='4ppo' size='340' side='right'caption='[[4ppo]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ppo]] 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=4PPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PPO 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]] 1.73&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PT:CYCLOHEXANE-1(R),2(R)-DIAMINE-PLATINUM(II)'>1PT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=4ppo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ppo OCA], [https://pdbe.org/4ppo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ppo RCSB], [https://www.ebi.ac.uk/pdbsum/4ppo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ppo 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 X-ray structure of the adduct formed between oxaliplatin and the model protein hen egg white lysozyme is reported here. The structure is compared with those of cisplatin and carboplatin derivatives, previously solved. Relevant changes are highlighted among these crystal structures that are suggestive of significant differences in the reactivity of platinum drugs with this protein; possible biological implications are discussed.


Authors: Messori, L., Merlino, A:
The X-ray structure of the complex formed in the reaction between oxaliplatin and lysozyme.,Messori L, Marzo T, Merlino A Chem Commun (Camb). 2014 Aug 7;50(61):8360-2. doi: 10.1039/c4cc02254h. PMID:24943911<ref>PMID:24943911</ref>


Description: First Crystal Structure for an Oxaliplatin-Protein Complex
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ppo" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Merlino A]]
[[Category: Messori L]]

Latest revision as of 20:20, 20 September 2023

First Crystal Structure for an Oxaliplatin-Protein ComplexFirst Crystal Structure for an Oxaliplatin-Protein Complex

Structural highlights

4ppo is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.73Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Publication Abstract from PubMed

The X-ray structure of the adduct formed between oxaliplatin and the model protein hen egg white lysozyme is reported here. The structure is compared with those of cisplatin and carboplatin derivatives, previously solved. Relevant changes are highlighted among these crystal structures that are suggestive of significant differences in the reactivity of platinum drugs with this protein; possible biological implications are discussed.

The X-ray structure of the complex formed in the reaction between oxaliplatin and lysozyme.,Messori L, Marzo T, Merlino A Chem Commun (Camb). 2014 Aug 7;50(61):8360-2. doi: 10.1039/c4cc02254h. PMID:24943911[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. ↑ Messori L, Marzo T, Merlino A. The X-ray structure of the complex formed in the reaction between oxaliplatin and lysozyme. Chem Commun (Camb). 2014 Aug 7;50(61):8360-2. doi: 10.1039/c4cc02254h. PMID:24943911 doi:http://dx.doi.org/10.1039/c4cc02254h

4ppo, resolution 1.73Å

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