Asset Details
Do you wish to reserve the book?
Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins
Do you wish to request the book?
Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins
2012
Overview
Proteins with similar crystal structures can have dissimilar rates of substrate binding and catalysis. Here we used molecular dynamics simulations and biochemical analysis to determine the role of intradomain and interdomain motions in conferring distinct activation rates to two Gα proteins, Gαi1 and GPA1. Despite high structural similarity, GPA1 can activate itself without a receptor, whereas Gαi1 cannot. We found that motions in these proteins vary greatly in type and frequency. Whereas motion is greatest in the Ras domain of Gαi1, it is greatest in helices αA and αB from the helical domain of GPA1. Using protein chimeras, we show that helix αA from GPA1 is sufficient to confer rapid activation to Gαi1. Gαi1 has less intradomain motion than GPA1 and instead displays interdomain displacement resembling that observed in a receptor–heterotrimer crystal complex. Thus, structurally similar proteins can have distinct atomic motions that confer distinct activation mechanisms.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Chimeras
/ GTP-Binding Protein alpha Subunits, Gi-Go
/ GTP-Binding Protein alpha Subunits, Gi-Go - chemistry
/ GTP-Binding Protein alpha Subunits, Gi-Go - metabolism
/ GTP-Binding Protein alpha Subunits, Gq-G11
/ GTP-Binding Protein alpha Subunits, Gq-G11 - chemistry
/ GTP-Binding Protein alpha Subunits, Gq-G11 - metabolism
/ Guanosine 5'-O-(3-Thiotriphosphate)
/ Guanosine 5'-O-(3-Thiotriphosphate) - chemistry
/ Guanosine 5'-O-(3-Thiotriphosphate) - metabolism
/ Kinetics
/ Molecular Dynamics Simulation
/ Protein Structure, Secondary
/ Proteins
