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Structure and function of ABC transporters.

Kenneth J Linton¹

¹MRC Clinical Sciences Centre, Imperial College Hammersmith Hospital Campus, London, United Kingdom. kenneth.linton@csc.mrc.ac.uk

Physiology (Bethesda, Md.)

|April 11, 2007

Summary

ATP binding cassette transporters are vital integral membrane proteins. Recent studies reveal their function through an ATP-switch model, crucial for cell physiology and disease.

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Area of Science:

Biochemistry
Molecular Biology
Cell Physiology

Background:

ATP binding cassette transporters are ubiquitous integral membrane proteins.
These transporters are critical for cell physiology, with clinical and economic importance.
Dysfunction is linked to genetic diseases and drug resistance.

Purpose of the Study:

To elucidate the functional mechanism of ATP binding cassette transporters.
To integrate structural and biochemical data for a comprehensive understanding.
To explain ligand translocation across biological membranes.

Main Methods:

Recent structure analyses of ATP binding cassette transporters.
Interpretation of structural data in the context of extensive biochemical studies.
Development of a functional model based on integrated data.

Main Results:

The ATP-switch model for transporter function has been proposed.
The model involves paired nucleotide binding domains switching conformations.
Conformational changes are dependent on ATP binding and hydrolysis.

Conclusions:

The ATP-switch model explains how ATP binding cassette transporters translocate ligands.
This model highlights the dynamic nature of these integral membrane proteins.
Understanding this mechanism is key to addressing related diseases and drug resistance.

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