Unlocking the eukaryotic membrane protein structural proteome

Most of the 231 unique membrane protein structures (as of 3/2010) are of bacterial membrane proteins (MPs) expressed in bacteria, or eukaryotic MPs from natural sources. However eukaryotic membrane proteins, especially those with more than three membrane crossings rarely succumb to any suitable expr...

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Bibliographic Details
Published in:Current opinion in structural biology 2010-08, Vol.20 (4), p.464-470
Main Authors: Lee, John Kyongwon, Stroud, Robert Michael
Format: Article
Language:English
Subjects:
Animals
Crystallization
Eukaryota - genetics
Green Fluorescent Proteins - genetics
HEK293 Cells
Humans
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Proteome - chemistry
Proteome - metabolism
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Summary:Most of the 231 unique membrane protein structures (as of 3/2010) are of bacterial membrane proteins (MPs) expressed in bacteria, or eukaryotic MPs from natural sources. However eukaryotic membrane proteins, especially those with more than three membrane crossings rarely succumb to any suitable expression in bacterial cells. They typically require expression in eukaryotic cells that can provide appropriate endoplasmic reticulum, chaperones, targeting and post-translational processing. In evidence, only ∼20 eukaryotic MP structures have resulted from heterologous expression. This is required for a general approach to target particular human or pathogen membrane proteins of importance to human health. The first of these appeared in 2005. Our review addresses the special issues that pertain to the expression of eukaryotic and human membrane proteins, and recent advances in the tool kit for crystallization and structure determination.
ISSN:0959-440X
1879-033X
DOI:10.1016/j.sbi.2010.05.004