Serotonin Transporter: Difference between revisions

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====Structure of SERTs====
====Structure of SERTs====
      SERTs are members of the sodium-coupled transporter family. These proteins harness the pre-existing sodium gradients to catalyze the uptake of serotonin.  Unfortunately, no high-resolution structure of a SERT has been solved. Instead a prokaryotic homolog of SERT, i.e. LeuT has been solved. LeuT shares significant sequence homology, especially for areas of the protein critical for function. The **overall structure of SERT** is dominated by alpha helices. A pore similar to that seen in the [[Potassium Channel]] **passes directly through** the structure. Serotonin passes through this pore upon reuptake. **Sodium ions stabilize** the serotonin bound structure before releasing serotonin within the presynaptic neuron.  
&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;SERTs are members of the sodium-coupled transporter family. These proteins harness the pre-existing sodium gradients to catalyze the uptake of serotonin.  Unfortunately, no high-resolution structure of a SERT has been solved. Instead a prokaryotic homolog of SERT, i.e. LeuT has been solved. LeuT shares significant sequence homology, especially for areas of the protein critical for function. The <scene name='Serotonin_Transporter/Helices/1'>overall structure of SERT</scene> is dominated by alpha helices. Serotonin passes through a <scene name='Serotonin_Transporter/Cavit/1'>central cavity</scene> upon reuptake. <scene name='Serotonin_Transporter/Sodium/1'>Sodium ions stabilize</scene> the serotonin bound structure before releasing serotonin within the presynaptic neuron.  


====Pharmaceutical Implications====
====Pharmaceutical Implications====