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1

Novel approach to computer modelling of seven-helical transmembrane proteins: Current progress in the test case of bacteriorhodopsin

100%
Nikiforovich G. V., Galaktionov S., Balodis J., Marshall G. R.
Acta Biochimica Polonica
|
2001
|
tom 48
|
nr 1
G-protein coupled receptors (GPCRs) are thought to be proteins with 7-membered transmembrane helical bundles (7TM proteins). Recently, the X-ray structures have been solved for two such proteins, namely for bacteriorhodopsin (BR) and rhodopsin (Rh), the latter being a GPCR. Despite similarities, the structures are different enough to suggest that 3D models for different GPCRs cannot be obtained directly employing 3D structures of BR or Rh as a unique template. The approach to computer modeling of 7TM proteins de­veloped in this work was capable of reproducing the experimental X-ray structure of BR with great accuracy. A combination of helical packing and low-energy conformers for loops most close to the X-ray structure possesses the r.m.s.d. value of 3.13 Ä. Such a level of accuracy for the 3D-structure prediction for a 216-residue protein has not been achieved, so far, by any available ab initio procedure of protein folding. The approach may produce also other energetically consistent combinations of helical bundles and loop con- formers, creating a variety of possible templates for 3D structures of 7TM proteins, in­cluding GPCRs. These templates may provide experimentalists with various plausible op­tions for 3D structure of a given GPCR; in our view, only experiments will determine the fi­nal choice of the most reasonable 3D template.
2

The Hippo pathway in colorectal cancer

84%
Wierzbicki P. M., Rybarczyk A.
Folia Histochemica et Cytobiologica
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2015
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tom 53
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nr 2
3
Content available remote

Membrane estrogen receptors - is it an alternative way of estrogen action?

67%
Soltysik K., Czekaj P.
Journal of Physiology and Pharmacology
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2013
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tom 64
|
nr 2
4

The functional antagonist Met-RANTES: a modified agonist that induces differential CCR5 trafficking

67%
Kiss D. L., Longden J., Fechner G. A., Avery V. M.
Cellular and Molecular Biology Letters
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2009
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tom 14
|
nr 4
537-547
CC chemokine receptor 5 (CCR5) is a pro-inflammatory chemokine receptor that is expressed on cells of the immune system, and specializes in cell migration in response to inflammation and tissue damage. Due to its key role in cell communication and migration, this receptor is involved in various inflammatory and autoimmune diseases, in addition to HIV infection. Met-RANTES is a modified CCR5 ligand that has previously been shown to antagonize CCR5 activation and function in response to its natural ligands in vitro. In vivo, Met-RANTES is able to reduce inflammation in models of induced inflammatory and autoimmune diseases. However, due to the fact that Met-RANTES is also capable of partial agonist activity regarding receptor signaling and internalization, it is clear that Met-RANTES does not function as a conventional receptor antagonist. To further elucidate the effect of Met-RANTES on CCR5, receptor trafficking was investigated in a CHO-CCR5-GFP cell line using the Opera confocal plate reader. The internalization response of CCR5 was quantified, and showed that Met-RANTES internalized CCR5 in a slower, less potent manner than the agonists CCL3 and CCL5. Fluorescent organelle labeling and live cell imaging showed CCL3 and CCL5 caused CCR5 to traffic through sorting endosomes, recycling endosomes and the Golgi apparatus. In contrast, Met-RANTES caused CCR5 to traffic through sorting endosomes and the Golgi apparatus in a manner that was independent of recycling endosomes. As receptor trafficking impacts on cell surface expression and the ability of the receptor to respond to more ligand, this information may indicate an alternative regulation of CCR5 by Met-RANTES that allows the modified ligand to reduce inflammation through stimulation of a pro-inflammatory receptor.
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