Sandbox 7726
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
| - | Mutation studies of the complex showed that highly conserved residues of CIC, W37, L40, and V41 display hydrophobic contacts with highly conserved residues of the AXH domain, V591, S602, and L686. These residues were found to be required for the PPI interaction as any combination mutation of these residues lead to the disruption of the PPI formation. | + | Mutation studies of the complex showed that highly conserved residues of CIC, <scene name='78/789347/Cic_impt_residues/2'>W37, L40, and V41</scene> display hydrophobic contacts with highly conserved residues of the AXH domain, V591, S602, and L686. These residues were found to be required for the PPI interaction as any combination mutation of these residues lead to the disruption of the PPI formation. |
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 06:32, 5 June 2018
Protein-protein interaction between Ataxin-1 and Capicua
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References
- ↑ Kim E, Lu HC, Zoghbi HY, Song JJ. Structural basis of protein complex formation and reconfiguration by polyglutamine disease protein Ataxin-1 and Capicua. Genes Dev. 2013 Mar 15;27(6):590-5. doi: 10.1101/gad.212068.112. PMID:23512657 doi:http://dx.doi.org/10.1101/gad.212068.112
