Study on functional sites in human multidrug resistance protein 1 (hMRP1)

Human multidrug resistance protein 1 (hMRP1) is an important member of the ATP‐binding cassette (ABC) transporter superfamily. It can extrude a variety of anticancer drugs and physiological organic anions across the plasma membrane, which is activated by substrate binding, and is accompanied by larg...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2021-06, Vol.89 (6), p.659-670
Hauptverfasser:	He, Junmei, Han, Zhongjie, Farooq, Qurat ul Ain, Li, Chunhua
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Allosteric properties Allosteric Site Animals Anions Antineoplastic drugs Antitumor agents Binding binding mode Cattle Domains Drug development Drug resistance Free energy Gaussian network model hMRP1 Homology Humans Hydrophobic and Hydrophilic Interactions Hydrophobicity Inflammation key residues Kinetics Leukotriene C4 - chemistry Leukotriene C4 - metabolism Molecular Docking Simulation Multidrug resistance Multidrug Resistance-Associated Proteins - chemistry Multidrug Resistance-Associated Proteins - metabolism Multidrug resistant organisms Nucleotides Perturbation Protein Binding Protein Conformation, alpha-Helical Protein Conformation, beta-Strand Protein Interaction Domains and Motifs Protein Isoforms - chemistry Protein Isoforms - metabolism Protein structure Proteins Residues Secondary structure Signal Transduction Static Electricity Structural Homology, Protein Substrate Specificity Substrates thermodynamic cycle Thermodynamics
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