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Related Concept Videos

ABC Transporters: Importer01:27

ABC Transporters: Importer

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ATP-binding cassette or ABC transporters are a class of ATP-driven pumps that hydrolyze ATP to move solutes across the membrane. They can be grouped into importers and exporters. While exporters are present in all domains of life, importers exist only in bacteria and some plants.
In bacteria, based on the number of transmembrane helices and the chemical nature of their substrates, the ABC importers can be divided into three types:
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ABC Transporters: Exporter01:31

ABC Transporters: Exporter

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ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Ligand Binding Sites02:40

Ligand Binding Sites

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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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The Significance of Membrane Transport01:44

The Significance of Membrane Transport

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The transport of solutes across the cell membrane is essential for metabolic processes, like maintaining cell size and volume, generating the action potential, exchanging nutrients and gases, etc. Membrane transport can be either passive or active. It can be simple diffusion, facilitated, or mediated transport aided by transport proteins such as transporters and channels.
Transporters facilitate either an active or passive movement of solutes. They can allow a single-molecule transport down its...
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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR
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Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

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Structural insights into binding-site access and ligand recognition by human ABCB1.

Devanshu Kurre1, Phuoc X Dang1,2, Le T M Le1,3

  • 1The Hormel Institute, University of Minnesota, Austin, MN, 55912, USA.

The EMBO Journal
|January 13, 2025
PubMed
Summary

Human ABCB1 efflux pump structures reveal how it transports diverse drugs. Understanding these mechanisms, particularly TM4 rearrangements, can guide the development of new multidrug resistance inhibitors.

Keywords:
ABC TransporterABCB1/MDR1/ p-glycoproteinMultidrug ResistanceStructural Biologycryo-EM

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Pharmacology

Background:

  • The ATP-binding cassette subfamily B member 1 (ABCB1) protein is crucial for drug transport and multidrug resistance.
  • The precise mechanisms by which ABCB1 recognizes and transports a wide array of substrates are not fully understood.

Purpose of the Study:

  • To elucidate the structural basis of ABCB1 substrate recognition and transport.
  • To investigate the conformational dynamics of ABCB1 in various functional states.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to determine high-resolution structures of lipid-embedded human ABCB1.
  • Structures were obtained in apo, substrate-bound, inhibitor-bound, and nucleotide-trapped states.

Main Results:

  • The substrate-binding site is located in one half of ABCB1 and is initially obstructed by transmembrane helix 4 (TM4).
  • Major transmembrane rearrangements, involving TM4, distinguish substrate and inhibitor binding.
  • Specific residues create localized flexibility and asymmetry within the transmembrane domains, influencing substrate binding.

Conclusions:

  • Structural insights into ABCB1 conformational changes and lipid interactions can predict substrate-binding profiles.
  • These findings provide a foundation for designing novel ABCB1 inhibitors to combat multidrug resistance.