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4ny5
From Proteopedia
(Difference between revisions)
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| - | + | ==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]] 1.85Å' scene=''> | |
| - | + | == 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Chick]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Merlino, A.]] | [[Category: Merlino, A.]] | ||
Revision as of 07:07, 7 May 2014
X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A
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Categories: Chick | Lysozyme | Merlino, A. | Messori, L. | Hydrolase | O-glycosyl
