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Mhp1 is a sodium dependent protein. The sodium binds at the C-terminal end of TM1a and interacts with TM8 (''Figure 2''). The dipole moment at the C-terminus of TM1a contributes to the binding.
Mhp1 is a sodium dependent protein. The sodium binds at the C-terminal end of TM1a and interacts with TM8 (''Figure 2''). The dipole moment at the C-terminus of TM1a contributes to the binding.


Experiments have shown that benzyl-hydantoin increases the affinity of sodium for Mhp1 and reciprocally sodium increases the affinity of benzyl-hydantoin for Mhp1. Therefore, the binding of the substrate and the cation are closely coupled.  
Experiments have shown that sodium increases the affinity of benzyl-hydantoin for Mhp1 and reciprocally benzyl-hydantoin increases the affinity of sodium for Mhp1.
Indeed, the presence of benzyl-hydantoin in Mhp1 binding site blocks the pathway of the sodium ion to the extracellular side. [doi: 10.1126/science.1186303]
Therefore, the binding of the substrate and the cation are closely coupled.  




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OCA, Morgane Diebold