4g49 - Revision history

OCA at 15:38, 14 March 2024

OCA — Thu, 14 Mar 2024 15:38:53 GMT

←Older revision		Revision as of 15:38, 14 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G49 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G49 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.4Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</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=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [https://pdbe.org/4g49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [https://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 ProSAT]</span></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=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [https://pdbe.org/4g49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [https://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== 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>		[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 anticancer complexes cisplatin and carboplatin are known to bind to both the Ndelta and the N atoms of His15 of hen egg-white lysozyme (HEWL) in the presence of dimethyl sulfoxide (DMSO). However, neither binds in aqueous media after 4 d of crystallization and crystal growth, suggesting that DMSO facilitates cisplatin/carboplatin binding to the N atoms of His15 by an unknown mechanism. Crystals of HEWL cocrystallized with cisplatin in both aqueous and DMSO media, of HEWL cocrystallized with carboplatin in DMSO medium and of HEWL cocrystallized with cisplatin and N-acetylglucosamine (NAG) in DMSO medium were stored for between seven and 15 months. X-ray diffraction studies of these crystals were carried out on a Bruker APEX II home-source diffractometer at room temperature. Room-temperature X-ray diffraction data collection removed the need for cryoprotectants to be used, ruling out any effect that the cryoprotectants might have had on binding to the protein. Both cisplatin and carboplatin still bind to both the Ndelta and N atoms of His15 in DMSO media as expected, but more detail for the cyclobutanedicarboxylate (CBDC) moiety of carboplatin was observed at the N binding site. However, two molecules of cisplatin were now observed to be bound to His15 in aqueous conditions. The platinum peak positions were identified using anomalous difference electron-density maps as a cross-check with Fo-Fc OMIT electron-density maps. The occupancies of each binding site were calculated using SHELXTL. These results show that over time cisplatin binds to both N atoms of His15 of HEWL in aqueous media, whereas this binding is speeded up in the presence of DMSO. The implication of cisplatin binding to proteins after a prolonged period of time is an important consideration for the length of treatment in patients who are given cisplatin.
-
-	Room-temperature X-ray diffraction studies of cisplatin and carboplatin binding to His15 of HEWL after prolonged chemical exposure.,Tanley SW, Schreurs AM, Kroon-Batenburg LM, Helliwell JR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1300-6., doi: 10.1107/S1744309112042005. Epub 2012 Oct 26. PMID:23143236<ref>PMID:23143236</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4g49" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 20:23, 19 October 2022

OCA — Wed, 19 Oct 2022 20:23:52 GMT

←Older revision		Revision as of 20:23, 19 October 2022
Line 3:		Line 3:
	<StructureSection load='4g49' size='340' side='right'caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4g49' size='340' side='right'caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4G49 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G49 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dd0\|4dd0]], [[4dd1\|4dd1]], [[4dd2\|4dd2]], [[4dd3\|4dd3]], [[4dd4\|4dd4]], [[4dd6\|4dd6]], [[4dd7\|4dd7]], [[4dd9\|4dd9]], [[4dda\|4dda]], [[4ddb\|4ddb]], [[4ddc\|4ddc]], [[4g4a\|4g4a]], [[4g4b\|4g4b]], [[4g4c\|4g4c]], [[4g4h\|4g4h]]</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=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [https://pdbe.org/4g49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [https://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [~~http~~://pdbe.org/4g49 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[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>	+	[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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 29:		Line 27:
	[[Category: Gallus gallus]]		[[Category: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Lysozyme]]~~	+	[[Category: Helliwell JR]]
-	[[Category: Helliwell~~, J R~~]]	+	[[Category: Kroon-Batenburg LMJ]]
-	[[Category: Kroon-Batenburg~~, L M.J~~]]	+	[[Category: Schreurs AMM]]
-	[[Category: Schreurs~~, A M.M~~]]	+	[[Category: Tanley SWM]]
-	[[Category: Tanley~~, S W.M]]~~	+
-	~~[[Category: Aqueous media]]~~	+
-	~~[[Category: Capillary]]~~	+
-	~~[[Category: Carboplatin]]~~	+
-	~~[[Category: Cisplatin]]~~	+
-	~~[[Category: Dmso media]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Omega scan data collection~~]]	+

OCA at 07:37, 27 March 2019

OCA — Wed, 27 Mar 2019 07:37:23 GMT

←Older revision		Revision as of 07:37, 27 March 2019
Line 1:		Line 1:

	==Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage==		==Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage==
-	<StructureSection load='4g49' size='340' side='right' caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>	+	<StructureSection load='4g49' size='340' side='right'caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G49 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G49 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dd0\|4dd0]], [[4dd1\|4dd1]], [[4dd2\|4dd2]], [[4dd3\|4dd3]], [[4dd4\|4dd4]], [[4dd6\|4dd6]], [[4dd7\|4dd7]], [[4dd9\|4dd9]], [[4dda\|4dda]], [[4ddb\|4ddb]], [[4ddc\|4ddc]], [[4g4a\|4g4a]], [[4g4b\|4g4b]], [[4g4c\|4g4c]], [[4g4h\|4g4h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dd0\|4dd0]], [[4dd1\|4dd1]], [[4dd2\|4dd2]], [[4dd3\|4dd3]], [[4dd4\|4dd4]], [[4dd6\|4dd6]], [[4dd7\|4dd7]], [[4dd9\|4dd9]], [[4dda\|4dda]], [[4ddb\|4ddb]], [[4ddc\|4ddc]], [[4g4a\|4g4a]], [[4g4b\|4g4b]], [[4g4c\|4g4c]], [[4g4h\|4g4h]]</td></tr>
Line 27:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Chick~~]]	+	[[Category: Gallus gallus]]
		+	[[Category: Large Structures]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
	[[Category: Helliwell, J R]]		[[Category: Helliwell, J R]]

OCA at 19:19, 4 August 2016

OCA — Thu, 04 Aug 2016 19:19:38 GMT

←Older revision		Revision as of 19:19, 4 August 2016
Line 1:		Line 1:
		+
	==Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage==		==Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage==
	<StructureSection load='4g49' size='340' side='right' caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>		<StructureSection load='4g49' size='340' side='right' caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dd0\|4dd0]], [[4dd1\|4dd1]], [[4dd2\|4dd2]], [[4dd3\|4dd3]], [[4dd4\|4dd4]], [[4dd6\|4dd6]], [[4dd7\|4dd7]], [[4dd9\|4dd9]], [[4dda\|4dda]], [[4ddb\|4ddb]], [[4ddc\|4ddc]], [[4g4a\|4g4a]], [[4g4b\|4g4b]], [[4g4c\|4g4c]], [[4g4h\|4g4h]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dd0\|4dd0]], [[4dd1\|4dd1]], [[4dd2\|4dd2]], [[4dd3\|4dd3]], [[4dd4\|4dd4]], [[4dd6\|4dd6]], [[4dd7\|4dd7]], [[4dd9\|4dd9]], [[4dda\|4dda]], [[4ddb\|4ddb]], [[4ddc\|4ddc]], [[4g4a\|4g4a]], [[4g4b\|4g4b]], [[4g4c\|4g4c]], [[4g4h\|4g4h]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [http://www.ebi.ac.uk/pdbsum/4g49 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [http://pdbe.org/4g49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [http://www.ebi.ac.uk/pdbsum/4g49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g49 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4g49" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 18:40, 24 December 2014

OCA — Wed, 24 Dec 2014 18:40:06 GMT

←Older revision		Revision as of 18:40, 24 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4g49.~~png~~\|~~left~~\|~~200px~~]]	+	==Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage==
		+	<StructureSection load='4g49' size='340' side='right' caption='[[4g49]], [[Resolution\|resolution]] 2.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4g49]] 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=4G49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G49 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPT:CISPLATIN'>CPT</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dd0\|4dd0]], [[4dd1\|4dd1]], [[4dd2\|4dd2]], [[4dd3\|4dd3]], [[4dd4\|4dd4]], [[4dd6\|4dd6]], [[4dd7\|4dd7]], [[4dd9\|4dd9]], [[4dda\|4dda]], [[4ddb\|4ddb]], [[4ddc\|4ddc]], [[4g4a\|4g4a]], [[4g4b\|4g4b]], [[4g4c\|4g4c]], [[4g4h\|4g4h]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g49 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g49 RCSB], [http://www.ebi.ac.uk/pdbsum/4g49 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The anticancer complexes cisplatin and carboplatin are known to bind to both the Ndelta and the N atoms of His15 of hen egg-white lysozyme (HEWL) in the presence of dimethyl sulfoxide (DMSO). However, neither binds in aqueous media after 4 d of crystallization and crystal growth, suggesting that DMSO facilitates cisplatin/carboplatin binding to the N atoms of His15 by an unknown mechanism. Crystals of HEWL cocrystallized with cisplatin in both aqueous and DMSO media, of HEWL cocrystallized with carboplatin in DMSO medium and of HEWL cocrystallized with cisplatin and N-acetylglucosamine (NAG) in DMSO medium were stored for between seven and 15 months. X-ray diffraction studies of these crystals were carried out on a Bruker APEX II home-source diffractometer at room temperature. Room-temperature X-ray diffraction data collection removed the need for cryoprotectants to be used, ruling out any effect that the cryoprotectants might have had on binding to the protein. Both cisplatin and carboplatin still bind to both the Ndelta and N atoms of His15 in DMSO media as expected, but more detail for the cyclobutanedicarboxylate (CBDC) moiety of carboplatin was observed at the N binding site. However, two molecules of cisplatin were now observed to be bound to His15 in aqueous conditions. The platinum peak positions were identified using anomalous difference electron-density maps as a cross-check with Fo-Fc OMIT electron-density maps. The occupancies of each binding site were calculated using SHELXTL. These results show that over time cisplatin binds to both N atoms of His15 of HEWL in aqueous media, whereas this binding is speeded up in the presence of DMSO. The implication of cisplatin binding to proteins after a prolonged period of time is an important consideration for the length of treatment in patients who are given cisplatin.

-	~~{{STRUCTURE_4g49\| PDB=4g49 \| SCENE= }}~~	+	Room-temperature X-ray diffraction studies of cisplatin and carboplatin binding to His15 of HEWL after prolonged chemical exposure.,Tanley SW, Schreurs AM, Kroon-Batenburg LM, Helliwell JR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Nov 1;68(Pt 11):1300-6., doi: 10.1107/S1744309112042005. Epub 2012 Oct 26. PMID:23143236<ref>PMID:23143236</ref>

-	~~===Room temperature X-ray diffraction~~ of ~~cisplatin binding to HEWL in aqueous media after 15 months~~ of ~~crystal storage===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23143236}}~~	+	==See Also==
-		+	*[[Lysozyme 3D structures\|Lysozyme 3D structures]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4g49~~]] ~~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=4G49 OCA].~~	+	<references/>
-	[[Category: ~~Gallus gallus~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Chick]]
	[[Category: Lysozyme]]		[[Category: Lysozyme]]
-	[[Category: Helliwell, J R.]]	+	[[Category: Helliwell, J R]]
-	[[Category: Kroon-Batenburg, L M.J.]]	+	[[Category: Kroon-Batenburg, L M.J]]
-	[[Category: Schreurs, A M.M.]]	+	[[Category: Schreurs, A M.M]]
-	[[Category: Tanley, S W.M.]]	+	[[Category: Tanley, S W.M]]
	[[Category: Aqueous media]]		[[Category: Aqueous media]]
	[[Category: Capillary]]		[[Category: Capillary]]

OCA at 11:43, 23 January 2013

OCA — Wed, 23 Jan 2013 11:43:42 GMT

←Older revision		Revision as of 11:43, 23 January 2013
Line 1:		Line 1:
-	[[Image:4g49.~~jpg~~\|left\|200px]]	+	[[Image:4g49.png\|left\|200px]]

	{{STRUCTURE_4g49\| PDB=4g49 \| SCENE= }}		{{STRUCTURE_4g49\| PDB=4g49 \| SCENE= }}
Line 5:		Line 5:
	===Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage===		===Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage===

		+	{{ABSTRACT_PUBMED_23143236}}

	==About this Structure==		==About this Structure==

OCA at 14:02, 8 November 2012

OCA — Thu, 08 Nov 2012 14:02:18 GMT

←Older revision		Revision as of 14:02, 8 November 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4g49.jpg\|left\|200px]]

-	~~The entry~~ 4g49 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4g49\| PDB=4g49 \| SCENE= }}

-	~~Authors: Tanley, S.W.M., Schreurs, A.M.M., Kroon~~-~~Batenburg, L.M.J., Helliwell, J.R.~~	+	===Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage===

-	~~Description~~: ~~Room temperature X~~-~~ray diffraction of cisplatin binding to HEWL in aqueous~~ media ~~after 15 months of crystal storage~~	+
		+	==About this Structure==
		+	[[4g49]] 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=4G49 OCA].
		+	[[Category: Gallus gallus]]
		+	[[Category: Lysozyme]]
		+	[[Category: Helliwell, J R.]]
		+	[[Category: Kroon-Batenburg, L M.J.]]
		+	[[Category: Schreurs, A M.M.]]
		+	[[Category: Tanley, S W.M.]]
		+	[[Category: Aqueous media]]
		+	[[Category: Capillary]]
		+	[[Category: Carboplatin]]
		+	[[Category: Cisplatin]]
		+	[[Category: Dmso media]]
		+	[[Category: Hydrolase]]
		+	[[Category: Omega scan data collection]]

OCA at 04:57, 8 August 2012

OCA — Wed, 08 Aug 2012 04:57:15 GMT

←Older revision		Revision as of 04:57, 8 August 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4g49 is ON HOLD	+	The entry 4g49 is ON HOLD until Paper Publication

	Authors: Tanley, S.W.M., Schreurs, A.M.M., Kroon-Batenburg, L.M.J., Helliwell, J.R.		Authors: Tanley, S.W.M., Schreurs, A.M.M., Kroon-Batenburg, L.M.J., Helliwell, J.R.

	Description: Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage		Description: Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage

OCA at 05:28, 1 August 2012

OCA — Wed, 01 Aug 2012 05:28:40 GMT

←Older revision		Revision as of 05:28, 1 August 2012
Line 3:		Line 3:
	The entry 4g49 is ON HOLD		The entry 4g49 is ON HOLD

-	Authors: Tanley, S.W.M, Schreurs, A.M.M, Kroon-Batenburg, L.M.J, Helliwell, J.R	+	Authors: Tanley, S.W.M., Schreurs, A.M.M., Kroon-Batenburg, L.M.J., Helliwell, J.R.

	Description: Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage		Description: Room temperature X-ray diffraction of cisplatin binding to HEWL in aqueous media after 15 months of crystal storage

OCA: Protected "4g49" [edit=sysop:move=sysop]

OCA — Wed, 25 Jul 2012 06:51:51 GMT

Protected "4g49" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:51, 25 July 2012