User:Alicia Daeden/Sandbox 130
From Proteopedia
The Solution Structure of Human Cardiac Troponin C in complex with the Green Tea Polyphenol; (-)-epigallocatechin-3-gallate
|
2KDH is a 1 chain structure of sequence from Homo sapiens. That is the PDB name for the solution structure of Human Cardiac Troponin C in complex with the green tea Polyphenol (-)-epigallocatechin-3-gallate.
Troponin C is a protein which can bind with calcium. That’s a subunit from a 3 subunited protein which is called Troponin. We find this protein in muscle.
Heart muscle contraction is regulated by Ca(2+) binding to the thin filament protein troponin C. In cardiovascular disease, the myofilament response to Ca(2+) is often altered. Compounds that rectify this perturbation are of considerable interest as therapeutics. Plant flavonoids have been found to provide protection against a variety of human illnesses such as cancer, infection, and heart disease. (-)-Epigallocatechin gallate (EGCg), the prevalent flavonoid in green tea is one of those plant flavonoids.
Structure & Function:
The troponin C is a part of the troponin complex which is composed of three proteins: the troponin C, troponin I and troponin T. The troponin C is involved in the process of muscular contraction. It can bind (with) the calcium and generates a change of conformation in the troponin complex. So the troponin I releases the site on the actin which can now bind (with) the myosin. Finally the muscular contraction is permitted. In some illnesses the fixation of the troponin C and the Calcium is altered like in Cancer, Infections or heart diseases. Some flavonoids as the flavonoid in green tea (EGCg) modulates force generation in isolated guinea pig hearts. EGCg binds (on) the C-terminal domain of troponin C–troponin I complex and has a cardiotonic effect. The properties were highlighted by several survey but we need to find a way to use it through drugs.
Interactions between the troponin C and the EGCg
The troponin C is a 72 residues protein organized with five helix and 2 sheets which are anti-parallel. There are which form an hydrophobic pocket.EGCg interracts with but there are 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 induces a small structural "opening". Image:EGCg.jpg
EGCg can bind the TnC-2Ca2+ or TnC-2Ca2+-TnI.
