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-TnC.jpg|350px]] '''''EGCg-TnC complex'''''[[Image:Pocket surface.jpg|350px]] | [[Image:EGC-TnC.jpg|350px]] '''''EGCg-TnC complex''''' | ||
[[Image:Pocket surface.jpg|350px]] '''''Pocket with a surface representation''''' | |||
As said just before, EGCg makes contacts exclusively to hydrophobic residues that line the surface of TnC. Actually it binds near the surface of helix E, so near the N-terminus of TnC, with tetrahydropyran and benzenediol. The pyrogallol ring stays near the C-terminus of TnC, which explains the large chemical shift perturbations of some residues of the <scene name='Human_Cardiac_Troponin_C/Helix_h/1'>Helix H</scene>. | As said just before, EGCg makes contacts exclusively to hydrophobic residues that line the surface of TnC. Actually it binds near the surface of helix E, so near the N-terminus of TnC, with tetrahydropyran and benzenediol. The pyrogallol ring stays near the C-terminus of TnC, which explains the large chemical shift perturbations of some residues of the <scene name='Human_Cardiac_Troponin_C/Helix_h/1'>Helix H</scene>. | ||