Inositol 1,4,5-Trisphosphate Receptor: Difference between revisions
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The α-domain of InsP<sub>3</sub>R shows a high degree of homology with an element called an armidillo repeat fold found in proteins such as β-catenin and importins.<ref name="mainpaper"/> In β-catenin and importins, the armadillo repeat functions as a motif for protein-protein interactions.<ref name="mainpaper"/> Within the α-domain of mouse InsP<sub>3</sub>R1, there are two large, highly conserved surfaces.<ref name="mainpaper"/> Both regions are rich in aromatic residues, indicating that they may function as interaction sites for parts of the receptor or other cellular proteins.<ref name="mainpaper"/> A possible option for this kind of binding domain would be the InsP<sub>3</sub> binding suppressor domain present at the N-terminus which reduces the binding affinity for the InsP<sub>3</sub> ligand.<ref name="mainpaper"/> | The α-domain of InsP<sub>3</sub>R shows a high degree of homology with an element called an armidillo repeat fold found in proteins such as β-catenin and importins.<ref name="mainpaper"/> In β-catenin and importins, the armadillo repeat functions as a motif for protein-protein interactions.<ref name="mainpaper"/> Within the α-domain of mouse InsP<sub>3</sub>R1, there are two large, highly conserved surfaces.<ref name="mainpaper"/> Both regions are rich in aromatic residues, indicating that they may function as interaction sites for parts of the receptor or other cellular proteins.<ref name="mainpaper"/> A possible option for this kind of binding domain would be the InsP<sub>3</sub> binding suppressor domain present at the N-terminus which reduces the binding affinity for the InsP<sub>3</sub> ligand.<ref name="mainpaper"/> | ||
[[Image:1n4k2.png|thumb|The two domains of the inositol 1,4,5-trisphosphate receptor protein. The yellow ribbons represent the β-domain and the red helices represent the α-domain]] | |||
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