Comparison of the transmembrane helices of bovine rhodopsin in the crystal structure and the C α template based on cryo-electron microscopy maps and sequence analysis of the G protein-coupled receptors

2002 ◽  
Vol 28 (8-9) ◽  
pp. 845-851 ◽  
Author(s):  
Siavoush Dastmalchi ◽  
Felix J. Kobus ◽  
Tiina P. Iismaa ◽  
Michael B. Morris ◽  
W. Bret Church
2002 ◽  
Vol 1565 (2) ◽  
pp. 168-182 ◽  
Author(s):  
R.E. Stenkamp ◽  
S. Filipek ◽  
C.A.G.G. Driessen ◽  
D.C. Teller ◽  
K. Palczewski

2020 ◽  
Vol 26 (1) ◽  
pp. 17-31
Author(s):  
Taiana Maia de Oliveira ◽  
Lotte van Beek ◽  
Fiona Shilliday ◽  
Judit É. Debreczeni ◽  
Chris Phillips

Single-particle cryogenic electron microscopy (cryo-EM) has been elevated to the mainstream of structural biology propelled by technological advancements in numerous fronts, including imaging analysis and the development of direct electron detectors. The drug discovery field has watched with (initial) skepticism and wonder at the progression of the technique and how it revolutionized the molecular understanding of previously intractable targets. This article critically assesses how cryo-EM has impacted drug discovery in diverse therapeutic areas. Targets that have been brought into the realm of structure-based drug design by cryo-EM and are thus reviewed here include membrane proteins like the GABAA receptor, several TRP channels, and G protein-coupled receptors, and multiprotein complexes like the ribosomes, the proteasome, and eIF2B. We will describe these studies highlighting the achievements, challenges, and caveats.


2004 ◽  
Vol 86 (4) ◽  
pp. 1904-1921 ◽  
Author(s):  
Rene J. Trabanino ◽  
Spencer E. Hall ◽  
Nagarajan Vaidehi ◽  
Wely B. Floriano ◽  
Victor W.T. Kam ◽  
...  

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