Sandbox PgpWWC
From Proteopedia
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==P-glycoprotein== | ==P-glycoprotein== | ||
<StructureSection load='4m1m' size='340' side='right' caption='P-glycoprotein: Both domains at 3.5 Å resolution ' scene=''> | <StructureSection load='4m1m' size='340' side='right' caption='P-glycoprotein: Both domains at 3.5 Å resolution ' scene=''> | ||
- | '''P-glycoprotein (P-gp, ABCB1)''' is an ATP casette transporter that hydrolyses ATP for conformational changes after a variety of substrates are transported. It is one of the membrane proteins responsible for the multi drug resistance (MDR) in cancer treatment, as well as various other drug therapies. <ref>Aller, S., Yu, J., Ward, A., Weng, Y., Chittaboina, S., Zhuo, R., . . . Chang, G. (2009). Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding. Science, 323(5922), 1718-1722. Retrieved April 4, 2015, from National Institutes of Health</ref><ref>He, L., & Liu, G. Q. (2002). Effects of various principles from Chinese herbal medicine on rhodamine123 accumulation in brain capillary endothelial cells. Acta Pharmacologica Sinica, 23(7), 591-596</ref> P-gp can be found in tumor cells, as well as in the liver, kidney, adrenal gland, intestine, blood-brain barrier (BBB), placenta, blood-testis barrier, and blood-ovarian barriers. An effective MDR transport protein, the high amount of active Pgp substrates stems from the polyspecificity for hydrophobic and aromatic compounds.<ref>Marchetti, S., Mazzanti, R., Beijnen, J. H., & Schellens, J. H. (2007). Concise review: clinical relevance of drug–drug and herb–drug interactions mediated by the ABC transporter ABCB1 (MDR1, P-glycoprotein). The Oncologist, 12(8), 927-941.</ref> | + | '''P-glycoprotein (P-gp, ABCB1)''' is an ATP casette transporter that hydrolyses ATP for conformational changes after a variety of substrates are transported. It is one of the membrane proteins responsible for the multi drug resistance (MDR) in cancer treatment, as well as various other drug therapies.<ref>Aller, S., Yu, J., Ward, A., Weng, Y., Chittaboina, S., Zhuo, R., . . . Chang, G. (2009). Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding. Science, 323(5922), 1718-1722. Retrieved April 4, 2015, from National Institutes of Health</ref><ref>He, L., & Liu, G. Q. (2002). Effects of various principles from Chinese herbal medicine on rhodamine123 accumulation in brain capillary endothelial cells. Acta Pharmacologica Sinica, 23(7), 591-596</ref> P-gp can be found in tumor cells, as well as in the liver, kidney, adrenal gland, intestine, blood-brain barrier (BBB), placenta, blood-testis barrier, and blood-ovarian barriers. An effective MDR transport protein, the high amount of active Pgp substrates stems from the polyspecificity for hydrophobic and aromatic compounds.<ref>Marchetti, S., Mazzanti, R., Beijnen, J. H., & Schellens, J. H. (2007). Concise review: clinical relevance of drug–drug and herb–drug interactions mediated by the ABC transporter ABCB1 (MDR1, P-glycoprotein). The Oncologist, 12(8), 927-941.</ref> |
{{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}} | {{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}} | ||
<scene name='69/699852/Hydrophobic_residues/4'>TextToBeDisplayed</scene> | <scene name='69/699852/Hydrophobic_residues/4'>TextToBeDisplayed</scene> |
Revision as of 16:03, 9 April 2015
P-glycoprotein
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References
- ↑ Aller, S., Yu, J., Ward, A., Weng, Y., Chittaboina, S., Zhuo, R., . . . Chang, G. (2009). Structure of P-Glycoprotein Reveals a Molecular Basis for Poly-Specific Drug Binding. Science, 323(5922), 1718-1722. Retrieved April 4, 2015, from National Institutes of Health
- ↑ He, L., & Liu, G. Q. (2002). Effects of various principles from Chinese herbal medicine on rhodamine123 accumulation in brain capillary endothelial cells. Acta Pharmacologica Sinica, 23(7), 591-596
- ↑ Marchetti, S., Mazzanti, R., Beijnen, J. H., & Schellens, J. H. (2007). Concise review: clinical relevance of drug–drug and herb–drug interactions mediated by the ABC transporter ABCB1 (MDR1, P-glycoprotein). The Oncologist, 12(8), 927-941.