Sandbox Reserved 1069: Difference between revisions

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'''Binding Site A'''
'''Binding Site A'''


<scene name='69/694236/Bsa/2'>Binding site A</scene> is in the center of the transmembrane domain, attached and confined via residues from the TM2 and TM5 helices. The TM2 helix has <scene name='69/694236/Bsa/4'>Asp45 and Asp49</scene>, and the TM5 has <scene name='69/694236/Bsa/5'>His153 and Asp157</scene>, which facilitate the binding and releasing of Zn<sup>2+</sup> within the sites. The TM5 helix is significantly shorter than the other 5 helices around it, and this length forms a cavity in the membrane. Site A is one of Yiip's active sites, where Zn<sup>2+</sup> is able to attach and eventually exit the cell via proton transport. This particular site has an ideal tetrahedron among its residues, which is preferred for Zn<sup>2+</sup> binding.
<scene name='69/694236/Bsa/2'>Binding site A</scene> is in the center of the transmembrane domain, attached and confined via residues from the TM2 and TM5 helices. The TM2 helix has <scene name='69/694236/Bsa/4'>Asp45 and Asp49</scene>, and the TM5 has <scene name='69/694236/Bsa/5'>His153 and Asp157</scene>, which facilitate the binding and releasing of Zn<sup>2+</sup> within the sites. The <scene name='69/694236/Shorttm5/1'>TM5 helix</scene> is significantly shorter than the other 5 helices around it, and this length forms a cavity in the membrane. Site A is one of Yiip's active sites, where Zn<sup>2+</sup> is able to attach and eventually exit the cell via proton transport. This particular site has an ideal tetrahedron among its residues, which is preferred for Zn<sup>2+</sup> binding.


[[Image:Binding_site_A.fw.png|200px|left|thumb|Figure 4. Binding Site A showing TM2 domain (left) and TM5 domain (right). The Asp45 and Asp49 as well as the His153 and Asp157 are the coordination residues in the acitve site]]
[[Image:Binding_site_A.fw.png|200px|left|thumb|Figure 4. Binding Site A showing TM2 domain (left) and TM5 domain (right). The Asp45 and Asp49 as well as the His153 and Asp157 are the coordination residues in the acitve site]]