4ny5: Difference between revisions

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-{{STRUCTURE_4ny5|  PDB=4ny5  |  SCENE=  }}
+==X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A==
-===X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A===
+<StructureSection load='4ny5' size='340' side='right' caption='[[4ny5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-{{ABSTRACT_PUBMED_24553967}}
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ny5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NY5 OCA]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RU:RUTHENIUM+ION'>RU</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j1a|4j1a]], [[4j1b|4j1b]]</td></tr>
+<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ny5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ny5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ny5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ny5 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A crystallographic study of the adduct formed between hen egg white lysozyme (HEWL) and NAMI-A, an established ruthenium(iii) anticancer agent in clinical trials, is presented here. The X-ray structure reveals that NAMI-A coordinates the protein, as a naked ruthenium ion, at two distinct sites (namely Asp101 or Asp119) after releasing all its original ligands (DMSO, imidazole and Cl(-)). Structural data of the HEWL/NAMI-A adduct are compared with those previously obtained for the HEWL adduct of AziRu, a NAMI-A analogue bearing a pyridine in place of imidazole. The present results further support the view that NAMI-A exerts its biological effects acting as a classical "prodrug" first undergoing activation and then causing extensive metalation of relevant protein targets. It is also proposed that the original Ru-ligands, although absent in the final adduct, play a major role in directing the ruthenium center to its ultimate anchoring site on the protein surface.
-==Function==
+Ruthenium metalation of proteins: the X-ray structure of the complex formed between NAMI-A and hen egg white lysozyme.,Messori L, Merlino A Dalton Trans. 2014 Mar 25;43(16):6128-31. doi: 10.1039/c3dt53582g. PMID:24553967<ref>PMID:24553967</ref>
-[[http://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>
-==About this Structure==
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-[[4ny5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NY5 OCA].
+</div>
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:024553967</ref><references group="xtra"/><references/>
+__TOC__
-[[Category: Gallus gallus]]
+</StructureSection>
+[[Category: Chick]]
 [[Category: Lysozyme]]
 [[Category: Merlino, A.]]