About: Crystals of Na /K -ATPase with bound cisplatin

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Crystals of Na /K -ATPase with bound cisplatin Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.sciencedirect.com/science/article/pii/S000629521400519X
Description	Cisplatin is the most widely used chemotherapeutics for cancer treatment, however, its administration is connected to inevitable adverse effects. Previous studies suggested that cisplatin is able to inhibit Na+/K+-ATPase (NKA), the enzyme responsible for maintaining electrochemical potential and sodium gradient across the plasma membrane. Here we report a crystallographic analysis of cisplatin bound to NKA in the ouabain bound E2P form. Despite a moderate resolution (7.4 angstrom and 7.9 angstrom), the anomalous scattering from platinum and a model representation from a recently published structure enabled localization of seven cisplatin binding sites by anomalous difference Fourier maps. Comparison with NKA structures in the E1P conformation suggested two possible inhibitory mechanisms for cisplatin. Binding to Met151 can block the N-terminal pathway for transported cations, while binding to Met171 can hinder the interaction of cytoplasmic domains during the catalytic cycle. Cisplatin is the most widely used chemotherapeutics for cancer treatment, however, its administration is connected to inevitable adverse effects. Previous studies suggested that cisplatin is able to inhibit Na+/K+-ATPase (NKA), the enzyme responsible for maintaining electrochemical potential and sodium gradient across the plasma membrane. Here we report a crystallographic analysis of cisplatin bound to NKA in the ouabain bound E2P form. Despite a moderate resolution (7.4 angstrom and 7.9 angstrom), the anomalous scattering from platinum and a model representation from a recently published structure enabled localization of seven cisplatin binding sites by anomalous difference Fourier maps. Comparison with NKA structures in the E1P conformation suggested two possible inhibitory mechanisms for cisplatin. Binding to Met151 can block the N-terminal pathway for transported cations, while binding to Met171 can hinder the interaction of cytoplasmic domains during the catalytic cycle. (en)
Title	Crystals of Na /K -ATPase with bound cisplatin Crystals of Na /K -ATPase with bound cisplatin (en)
skos:prefLabel	Crystals of Na /K -ATPase with bound cisplatin Crystals of Na /K -ATPase with bound cisplatin (en)
skos:notation	RIV/61989592:15310/14:33150766!RIV15-MSM-15310___
http://linked.open...avai/riv/aktivita	P S
http://linked.open...avai/riv/aktivity	P(LO1204), S
http://linked.open...iv/cisloPeriodika	3
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Kubala, Martin Huličiak, Miroslav
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	9314
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/14:33150766
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	X-ray crystallography; Sodium pump; Na+/K+-ATPase; Cisplatin; Binding sites; Adverse effects (en)
http://linked.open.../riv/klicoveSlovo	Cisplatin X-ray crystallography Binding sites Adverse effects Na+/K+-ATPase Sodium pump
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[1B7E545F2845]
http://linked.open...i/riv/nazevZdroje	Biochemical Pharmacology
http://linked.open...in/vavai/riv/obor	BO
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	6 (xsd:int)
http://linked.open...vavai/riv/projekt	Udržitelný rozvoj výzkumu v Centru regionu Haná
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	92
http://linked.open...iv/tvurceVysledku	Kubala, Martin Huličiak, Miroslav Nissen, Poul Fedosova, Natalya Laursen, Mette Reinhard, Linda
http://linked.open...ain/vavai/riv/wos	000345955400010
issn	0006-2952
number of pages	5 (xsd:int)
http://bibframe.org/vocab/doi	10.1016/j.bcp.2014.08.029
http://localhost/t...ganizacniJednotka	15310

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 91 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software