Home > Articles > Published articles > The role of Cysteine 6.47 in class A GPCRs |
Date: | 2013 |
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. |
Rights: | Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. |
Language: | Anglès |
Document: | Article ; Versió publicada |
Published in: | BMC Structural biology, Vol. 13, Núm. 3 (March 2013) , p. 1-10, ISSN 1472-6807 |
11 p, 2.4 MB |
Additional file 1 1073x3090, 430.9 KB |