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T-shaped arrangement of the recombinant agrin G3–IgG Fc protein

Patel, T. R., Meier, M., Li, J., Morris, Gordon, Rowe, A. J. and Stetefeld, J. (2011) T-shaped arrangement of the recombinant agrin G3–IgG Fc protein. Protein Science, 20 (6). pp. 931-940. ISSN 0961-8368

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Abstract

Agrin is a large heparin sulphate proteoglycan with multiple domains, which is located in the extracellular matrix. The C-terminal G3 domain of agrin is functionally one of the most important domains. It harbors an α-dystroglycan binding site and carries out acetylcholine receptor clustering activities. In the present study, we have fused the G3 domain of agrin to an IgG Fc domain to produce a G3-Fc fusion protein that we intend to use as a tool to investigate new binding partners of agrin. As a first step of the study, we have characterized the recombinant fusion protein using a multidisciplinary approach using dynamic light scattering, analytical ultracentrifugation and small angle X-ray scattering (SAXS). Interestingly, our SAXS analysis using the high-resolution structures of G3 and Fc domain as models indicates that the G3-Fc protein forms a T-shaped molecule with the G3 domains extruding perpendicularly from the Fc scaffold. To validate our models, we have used the program HYDROPRO to calculate the hydrodynamic properties of the solution models. The calculated values are in excellent agreement with those determined experimentally

Item Type: Article
Subjects: Q Science > QD Chemistry
Schools: School of Applied Sciences
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Depositing User: Gordon Morris
Date Deposited: 26 May 2011 16:10
Last Modified: 26 May 2011 16:10
URI: http://eprints.hud.ac.uk/id/eprint/10613

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