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The catalytic cycle of P‐glycoprotein
Abstract
P‐glycoprotein is a plasma‐membrane glycoprotein which confers multidrug‐resistance on cells and displays ATP‐driven drug‐pumping in vitro. It contains two nucleotide‐binding domains, and its structure places it in the ‘ABC transporter’ family. We review recent evidence that both nucleotide‐sites bind and hydrolyse Mg‐ATP. The two catalytic sites interact strongly. A minimal scheme for the MgATP hydrolysis reaction is presented. An alternating catalytic sites scheme is proposed, in which drug transport is coupled to relaxation of a high‐energy catalytic site conformation generated by the hydrolysis step. Other ABC transporters may show similar catalytic features.
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Cited by
Microbial Cellulose Utilization: Fundamentals and Biotechnology
Lynd, L. R., Weimer, P. J., van Zyl, W. H., & Pretorius, I. S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.3.506-577.2002 · Cited by 4,726
Deeley, R. G., Westlake, C., & Cole, S. P. C. (2006) · Physiological Reviews · doi:10.1152/physrev.00035.2005 · Cited by 761
ABC transporters: physiology, structure and mechanism – an overview
Higgins, C. F. (2001) · Research in Microbiology · doi:10.1016/s0923-2508(01)01193-7 · Cited by 641
Toward Understanding the Assembly and Structure of KATPChannels
AGUILAR-BRYAN, L., CLEMENT, J. P., GONZALEZ, G., KUNJILWAR, K., BABENKO, A., & BRYAN, J. (1998) · Physiological Reviews · doi:10.1152/physrev.1998.78.1.227 · Cited by 540
Modulation of P-glycoprotein efflux pump: induction and activation as a therapeutic strategy
Silva, R., Vilas-Boas, V., Carmo, H., Dinis-Oliveira, R. J., Carvalho, F., de Lourdes Bastos, M., & Remião, F. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.11.013 · Cited by 339
Metadata
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1995-12-27
- Volume
- 377
- Issue
- 3
- Pages
- 285-289
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1994265289
- Cited by
- 440
- References
- 0
- FWCI
- 5.45
- Type
- journal article
- Language
- en
- Open access
- closed
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