کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2029972 | 1070995 | 2010 | 11 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Conformational Changes in Guanylate Cyclase-Activating Protein 1 Induced by Ca2+ and N-Terminal Fatty Acid Acylation Conformational Changes in Guanylate Cyclase-Activating Protein 1 Induced by Ca2+ and N-Terminal Fatty Acid Acylation](/preview/png/2029972.png)
SummaryNeuronal Ca2+ sensors (NCS) are high-affinity Ca2+-binding proteins critical for regulating a vast range of physiological processes. Guanylate cyclase-activating proteins (GCAPs) are members of the NCS family responsible for activating retinal guanylate cyclases (GCs) at low Ca2+ concentrations, triggering synthesis of cGMP and recovery of photoreceptor cells to the dark-adapted state. Here we use amide hydrogen-deuterium exchange and radiolytic labeling, and molecular dynamics simulations to study conformational changes induced by Ca2+ and modulated by the N-terminal myristoyl group. Our data on the conformational dynamics of GCAP1 in solution suggest that Ca2+ stabilizes the protein but induces relatively small changes in the domain structure; however, loss of Ca+2 mediates a significant global relaxation and movement of N- and C-terminal domains. This model and the previously described “calcium-myristoyl switch” proposed for recoverin indicate significant diversity in conformational changes among these highly homologous NCS proteins with distinct functions.
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Journal: - Volume 18, Issue 1, 13 January 2010, Pages 116–126