User:Mark Macbeth/Sandbox4: Difference between revisions
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== Structure == | == Structure == | ||
<StructureSection load='2i2y' size='400' side='right' caption='SRp20 bound to RNA ligand | <StructureSection load='2i2y' size='400' side='right' caption='SRp20 bound to RNA ligand' scene='78/782597/Rrmredgreen/2'> | ||
=== Structure Determination === | === Structure Determination === | ||
Attempts to determine the structure of native SRp20 have been largely unsuccessful due to the low solubility of the protein. This is likely due to the hydrophobic core of the RRM and exposed hydrophobic residues for RNA recognition on the β-sheets. As a solution, researchers removed the SR domain from the C terminus, leaving only the SRp20 RRM and a small arginine rich segment at the C terminus, then fused with a soluble <scene name='78/782597/Imager0/2'>IgG binding domain</scene> of Streptococcal protein G to the N terminus of the protein, providing the first published structure of the SRp20 RRM via NMR. However, the solution of the structure via [https://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR], in addition to fusion with a globular tag, results in multiple possible conformations of the protein, meaning measurements such as bond angles, lengths, and substrate interactions are variable. Further, information concerning structural aspects of the SR domain are still limited to experimental data of protein function with certain mutations or deletions, and by comparison to sister proteins such as 9G8. To date, structure of the SR domain or the protein without the globular tag have not been solved, nor has a crystal structure for any part of the protein been determined<ref name="Hargous">PMID:17036044</ref>. | Attempts to determine the structure of native SRp20 have been largely unsuccessful due to the low solubility of the protein. This is likely due to the hydrophobic core of the RRM and exposed hydrophobic residues for RNA recognition on the β-sheets. As a solution, researchers removed the SR domain from the C terminus, leaving only the SRp20 RRM and a small arginine rich segment at the C terminus, then fused with a soluble <scene name='78/782597/Imager0/2'>IgG binding domain</scene> of Streptococcal protein G to the N terminus of the protein, providing the first published structure of the SRp20 RRM via NMR. However, the solution of the structure via [https://en.wikipedia.org/wiki/Nuclear_magnetic_resonance NMR], in addition to fusion with a globular tag, results in multiple possible conformations of the protein, meaning measurements such as bond angles, lengths, and substrate interactions are variable. Further, information concerning structural aspects of the SR domain are still limited to experimental data of protein function with certain mutations or deletions, and by comparison to sister proteins such as 9G8. To date, structure of the SR domain or the protein without the globular tag have not been solved, nor has a crystal structure for any part of the protein been determined<ref name="Hargous">PMID:17036044</ref>. | ||
