Human Cardiac Troponin C: Difference between revisions
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There are <scene name='Human_Cardiac_Troponin_C/Hydrophobic/2'>hydrophobic residues</scene> which form an hydrophobic pocket.EGCg interacts with AC3 hydrophobic domain of the molecule and binds with AC2 domain. But there are <scene name='Human_Cardiac_Troponin_C/Residues_of_beta-sheet/1'>some residues of beta-sheet</scene> wich have no interactions with that molecule and this suggets that the binding of EGCg is near of the hydrophobic pocket rather than deep within the pocket and it induces a small structural "opening". The opening degree of TnC is described by the inter-helical angles between helices E and F and between helices G and H. | There are <scene name='Human_Cardiac_Troponin_C/Hydrophobic/2'>hydrophobic residues</scene> which form an hydrophobic pocket.EGCg interacts with AC3 hydrophobic domain of the molecule and binds with AC2 domain. But there are <scene name='Human_Cardiac_Troponin_C/Residues_of_beta-sheet/1'>some residues of beta-sheet</scene> wich have no interactions with that molecule and this suggets that the binding of EGCg is near of the hydrophobic pocket rather than deep within the pocket and it induces a small structural "opening". The opening degree of TnC is described by the inter-helical angles between helices E and F and between helices G and H. | ||
[[Image:EGC-TnC2.jpg|300px|Figure 1: EGCg-TnC complex]] | [[Image:EGC-TnC2.jpg|300px|left|thumb|Figure 1: EGCg-TnC complex]] | ||
[[Image:Pocket surface.jpg|300px|Pocket with a surface representation]] | [[Image:Pocket surface.jpg|300px|right|thumb|Figure 2: Pocket with a surface representation]] | ||
[[Image:1dqa opening.png|300px|left|thumb| Human HMG-CoA Reductase Catalytic Domain, [[1dqa]]]] | [[Image:1dqa opening.png|300px|left|thumb| Human HMG-CoA Reductase Catalytic Domain, [[1dqa]]]] | ||