| dc.contributor |
Universitat de Vic. Escola Politècnica Superior |
| dc.contributor |
Universitat de Vic. Grup de Recerca en Bioinformàtica i Estadística Mèdica |
| dc.contributor.author |
Olivella, Mireia |
| dc.contributor.author |
Caltabiano, Gianluigi |
| dc.contributor.author |
Cordomí Montoya, Arnau |
| dc.date |
2013 |
| dc.identifier |
Olivella, M., Caltabiano, G. & Cordomi, A. 2013, "The role of Cysteine 6.47 in class A GPCRs", Bmc Structural Biology, vol. 13, pp. 3. |
| dc.identifier |
1472-6807 |
| dc.identifier.uri |
http://hdl.handle.net/10854/2218 |
| dc.description |
Abstract
Background: The CWxP motif of transmembrane helix 6 (x: any residue) is highly conserved in class A GPCRs.
Within this motif, W6.48 is a big star in the theory of the global “toggle switch” because of its key role in the
activation mechanism of GPCRs upon ligand binding. With all footlights focused on W6.48, the reason why the
preceding residue, C6.47, is largely conserved is still unknown. The present study is aimed to fill up this lack of
knowledge by characterizing the role of C6.47 of the CWxP motif.
Results: A complete analysis of available crystal structures has been made alongside with molecular dynamics
simulations of model peptides to explore a possible structural role for C6.47.
Conclusions: We conclude that C6.47 does not modulate the conformation of the TM6 proline kink and propose
that C6.47 participates in the rearrangement of the TM6 and TM7 interface accompanying activation. |
| dc.format |
application/pdf |
| dc.language |
eng |
| dc.publisher |
Biomed Central |
| dc.relation |
http://www.biomedcentral.com/1472-6807/13/3 |
| dc.rights |
Aquest document està subjecte a aquesta llicència Creative Commons |
| dc.rights |
http://creativecommons.org/licenses/by-nc-nd/3.0/es/ |
| dc.rights |
info:eu-repo/semantics/openAccess |
| dc.subject |
Proteïnes |
| dc.title |
The role of Cysteine 6.47 in class A GPCRs |
| dc.type |
info:eu-repo/semantics/article |
| dc.type |
info:eu-repo/publishedVersion |
