The recombinant expression systems for structure determination of eukaryotic membrane proteins
Рекомбинантные системы экспрессии для определения структуры эукариотических мембранных белков
2014-08-14
SCID: 54.1/22j59s4g
Discuss with AI
eukaryotic membrane proteinsmembrane protein structure determinationprotein crystallizationprotein purificationrecombinant expression systems
Figures from the paper
Abstract (AI)
Eukaryotic membrane proteins, many of which are key players in various biological processes, constitute more than half of the drug targets and represent important candidates for structural studies. In contrast to their physiological significance, only very limited number of eukaryotic membrane protein structures have been obtained due to the technical challenges in the generation of recombinant proteins. In this review, we examine the major recombinant expression systems for eukaryotic membrane proteins and compare their relative advantages and disadvantages. We also attempted to summarize the recent technical strategies in the advancement of eukaryotic membrane protein purification and crystallization.
Key Findings
1
Eukaryotic membrane proteins are biologically important and account for more than half of drug targets, yet relatively few structures have been determined.
2
Recent technical strategies for improving eukaryotic membrane protein purification and crystallization are summarized.
3
The limited structural characterization of eukaryotic membrane proteins is primarily constrained by technical difficulties in generating suitable recombinant proteins.
4
The review compares major recombinant expression systems for eukaryotic membrane proteins, outlining their relative advantages and disadvantages.
Research Object
recombinant expression systems for eukaryotic membrane proteins
Research Subject
the relative advantages and disadvantages of these expression systems, along with strategies for eukaryotic membrane protein purification and crystallization for structure determination
Publication Details
Publication Date
2014-08-14
Journal
Publisher
ISSN
Open access PDF
Access Type
Author Information
Download PDF
Subscribe to digest