Human Cardiac Troponin C: Difference between revisions

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[[Image:EGC-TnC2.jpg|300px|Figure 1: EGCg-TnC complex]]  
[[Image:EGC-TnC2.jpg|300px|Figure 1: EGCg-TnC complex]]  
[[Image:Pocket surface.jpg|300px|Pocket with a surface representation]]  
[[Image:Pocket surface.jpg|300px|Pocket with a surface representation]]  
[[Image:1dqa opening.png|300px|left|thumb| Human HMG-CoA Reductase Catalytic Domain, [[1dqa]]]]


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>.

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Alicia Daeden, Céline Challemel, Audrey Chabrat, Michal Harel