<p>This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</p> <p>Membrane proteins (MPs) are responsible for the interface between the exterior and the interior of the cell. These proteins are implicated in numerous diseases,
such as cancer, cystic fibrosis, epilepsy, hyperinsulinism, heart failure, hypertension
and Alzheimer's disease. However, studies on these disorders are hampered by
a lack of structural information about the proteins involved. Structural analysis
requires large quantities of pure and active proteins. The majority of medically and
pharmaceutically relevant MPs are present in tissues at very low concentration, which
makes heterologous expression in large-scale production-adapted cells a prerequisite
for structural studies. Obtaining mammalian MP structural data depends on the
development of methods that allow the production of large quantities of MPs.
This review focuses on the different heterologous expression systems, and the
purification strategies, used to produce large amounts of pure mammalian MPs for
structural proteomics.</p>
[]
Comp Funct Genomics. 2002 Dec; 3(6):511-517