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Scripps Research scientists solve mystery of nerve disease genes
Date:7/4/2011

obtain the structures of five different GlyRS mutants and the wild-type protein in solution. This method, called hydrogendeuterium exchange, gives information about which parts of a protein are in touch with a solutionin other words, which parts lie on the outside rather than being buried deep inside its three-dimensional shape. In collaboration with Min Guo, assistant professor at Scripps Florida, a second method, called small angle X-ray scattering, was used to measure changes in the overall shape of the protein structure in solution.

Together, the results revealed that every GARS mutation studied causes a structural opening in the resulting mutant protein. By superimposing the information obtained from the structures in solution to the high-resolution X-ray crystal structure of the wild-type GlyRS protein, Yang, He, Zhang and colleagues were able to determine that the structural opening maps to a common region of the GlyRS protein in all the mutants.

By becoming more open to potential new partners, the GlyRS mutants may gain a new function that is toxic to nerve cells. That would explain why CMT type 2D is inherited in a dominant fashion.

Exciting Implications

The team is now looking for proteins that might bind to this region and already have leads on several candidates. As exciting as this work is, says He, "this paper is just the start of the story; we have more story coming, and it's getting more and more exciting."

This disease mechanism may also apply to other conditions. "Some proteins may be relatively unstable and can be easily triggered into another conformation by different types of mutations," explained Yang. "This example deals with the GlyRS protein, but the general idea can be applied to many other mutation-induced human diseases."

One example may be ALS. Some inherited forms of ALS are caused in a gene that encodes the enzyme copper-zinc superoxide dismutase (commonly called SOD1). To da
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Contact: Mika Ono
mikaono@scripps.edu
858-784-2052
Scripps Research Institute
Source:Eurekalert

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