User:Wayne Decatur/Sandbox Glutamate receptor: Difference between revisions

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Wayne Decatur (talk | contribs)
Wayne Decatur (talk | contribs)
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*The segments shown again, <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Transmem/4'>this time parallel to the four-fold axis</scene>.
*The segments shown again, <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Transmem/4'>this time parallel to the four-fold axis</scene>.
::There is <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Transmemclosed/1'>no pore visible in the center</scene> consistent with the channel being in a closed state with the antagonist (ZK200775) bound to the LBD.
::There is <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/Transmemclosed/1'>no pore visible in the center</scene> consistent with the channel being in a closed state with the antagonist (ZK200775) bound to the LBD.
::It is <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/M3_closed/2'>the tight helix crossing of specifically the M3 helices</scene> that occludes the channel. [BE PATIENT as a small surface is generated.]
::It is <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/M3_closed/3'>the tight helix crossing of specifically the M3 helices</scene> that occludes the channel. [BE PATIENT as a small surface is generated.]
::Note <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/M3_closed_top/1'>the differences between the conformations of the carboxy-termini ('top') of the subunit A/C and B/D M3 segments</scene>. This is in part is why the symmetry is only approximately four-fold and is one of the several intriguing observations in regard to symmetry for this macromolecule. In fact, the location of two-fold symmetry at the ends of M3 is just above the portion that spans the membrane and is close to the last region of the structure that doesn't show four-fold symmetry as abruptly below this point everything is four-fold symmetric.
::Note <scene name='User:Wayne_Decatur/Sandbox_Glutamate_receptor/M3_closed_top/1'>the differences between the conformations of the carboxy-termini ('top') of the subunit A/C and B/D M3 segments</scene>. This is in part is why the symmetry is only approximately four-fold and is one of the several intriguing observations in regard to symmetry for this macromolecule. In fact, the location of two-fold symmetry at the ends of M3 is just above the portion that spans the membrane and is close to the last region of the structure that doesn't show four-fold symmetry as abruptly below this point everything is four-fold symmetric.