Báo cáo y học: "Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5)"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: "Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5) | Theoretical Biology and Medical Modelling BioMed Central Research Molecular model of the outward facing state of the human P-glycoprotein ABCB1 and comparison to a model of the human MRP5 AbCC5 Aina W Ravna Ingebrigt Sylte and Georg Sager Open Access Address Department of Pharmacology Institute of Medical Biology University of Tromso N-9037 Tromso Norway Email Aina W Ravna - Ingebrigt Sylte - Georg Sager - Corresponding author Published 6 September 2007 Received 2 July 2007 Theoretical Biology and Medical Modelling 2007 4 33 doi 1742-4682-4-33 Accepted 6 September 2007 This article is available from http content 4 1 33 2007 Ravna et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract__ Background Multidrug resistance is a particular limitation to cancer chemotherapy antibiotic treatment and HIV medication. The ABC ATP binding cassette transporters human P-glycoprotein ABCB1 and the human MRP5 ABCC5 are involved in multidrug resistance. Results In order to elucidate structural and molecular concepts of multidrug resistance we have constructed a molecular model of the ATP-bound outward facing conformation of the human multidrug resistance protein ABCBI using the SavI866 crystal structure as a template and compared the ABCBI model with a previous ABCC5 model. The electrostatic potential surface EPS of the ABCBI substrate translocation chamber which transports cationic amphiphilic and lipophilic substrates was neutral with negative and weakly positive areas. In contrast EPS of the ABCC5 substrate translocation chamber which transports

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