ArticleProtein science : a publication of the Protein Society2011
T-shaped arrangement of the recombinant agrin G3-IgG Fc protein.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Human DDX17 Unwinds Rift Valley Fever Virus Non-Coding RNAs.International journal of molecular sciences · 2020Article
- Structural and Hydrodynamic Characterization of Dimeric Human Oligoadenylate Synthetase 2.Biophysical journal · 2020Article
- Nanoscale Structure Determination of Murray Valley Encephalitis and Powassan Virus Non-Coding RNAs.Viruses · 2020Article
- Interaction studies of a protein and carbohydrate system using an integrated approach: a case study of the miniagrin-heparin system.European biophysics journal : EBJ · 2018Article
- Impact of the structural integrity of the three-way junction of adenovirus VAI RNA on PKR inhibition.PloS one · 2017Article
- Dynamic light scattering: a practical guide and applications in biomedical sciences.Biophysical reviews · 2016Review
- Recognition of viral RNA stem-loops by the tandem double-stranded RNA binding domains of PKR.RNA (New York, N.Y.) · 2013Article
- Influence of the cosolute environment on IgG solution structure analyzed by small-angle X-ray scattering.The journal of physical chemistry. B · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.