Atropine: Difference between revisions

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The protein structure of an acetycholine receptor can be seen on the right. Although there is not a PDB ID for atropine in complex with the acetylcholine receptor, it is important to understand the structure of the acetylcholine receptor, and subsequently, how atropine and other alkaloids interact with it. One can see that each color in the current model represents a portion of the complex protien, which contains five domains. The <scene name='Sandbox_53/Achr_hydrophobicity/1'>hydrophobic</scene> regions can then be displayed in gray, while the hydrophillic regions appear purple. This shows a transmembrane alpha-helix region in the center of the molecule, a large hydrophillic complex on the exoplasmic face of the protein, and another hydrophillic region on the cystolic face of the protein. By highlighting the <scene name='Sandbox_53/Achr_secondarystructure/1'>secondary structure</scene> of the acetylcholine receptor, it is also easy to see how the secondary structure is concentrated to specific regions of the molecule. Alpha helicies span the majority of the transmembrane and cystolic regions, and beta sheets (with the exception of only a few alpha helicies) make up the majority of the exoplasmic receptor face. Atropine interacts with the <scene name='Sandbox_53/Achr_activesite/1'>residues</scene> of the exoplasmic face. It interacts so well, it is actually considered to be a "pure antagonist" by some <ref>Parker, Julie C; Sarkar, Deboshree; Quick, Michael W; Lester, Robin A. ''Interactions of Atropine with heterologously expressed and native alpha3 subunit-containing nicotinic acetylcholine receptors''. British Journal of Pharmacology. 138:5. p801-810. 2009. </ref>.

Atropine first enters the acetylcholine receptor and binds to the <scene name='Sandbox_53/Achr_activesite/1'>residues</scene> at the top of the receptor. They then interact with the,<scene name='Sandbox_53/Achr_residues/1'>val 255 and leu 251</scene> residues which define a hydrophobic region through which a dehydrated ion could pass through.

Atropine first enters the acetylcholine receptor and binds to the <scene name='Sandbox_53/Achr_activesite/1'>residues</scene> at the top of the receptor. They then interact with the,<scene name='Sandbox_53/Achr_residues/1'>val 255 and leu 251</scene> residues which define a hydrophobic region through which a dehydrated ion could pass through. These residues can be seen more clearly through this <scene name='Sandbox_53/Achr_residues2/1'>contacts</scene> representation.

The interaction of atropine and phospholipase 2A will be discussed in detail later in this article.

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 The protein structure of an acetycholine receptor can be seen on the right. Although there is not a PDB ID for atropine in complex with the acetylcholine receptor, it is important to understand the structure of the acetylcholine receptor, and subsequently, how atropine and other alkaloids interact with it. One can see that each color in the current model represents a portion of the complex protien, which contains five domains. The <scene name='Sandbox_53/Achr_hydrophobicity/1'>hydrophobic</scene> regions can then be displayed in gray, while the hydrophillic regions appear purple. This shows a transmembrane alpha-helix region in the center of the molecule, a large hydrophillic complex on the exoplasmic face of the protein, and another hydrophillic region on the cystolic face of the protein. By highlighting the <scene name='Sandbox_53/Achr_secondarystructure/1'>secondary structure</scene> of the acetylcholine receptor, it is also easy to see how the secondary structure is concentrated to specific regions of the molecule. Alpha helicies span the majority of the transmembrane and cystolic regions, and beta sheets (with the exception of only a few alpha helicies) make up the majority of the exoplasmic receptor face. Atropine interacts with the <scene name='Sandbox_53/Achr_activesite/1'>residues</scene> of the exoplasmic face. It interacts so well, it is actually considered to be a "pure antagonist" by some <ref>Parker, Julie C; Sarkar, Deboshree; Quick, Michael W; Lester, Robin A. ''Interactions of Atropine with heterologously expressed and native alpha3 subunit-containing nicotinic acetylcholine receptors''. British Journal of Pharmacology. 138:5. p801-810. 2009. </ref>.
-Atropine first enters the acetylcholine receptor and binds to the <scene name='Sandbox_53/Achr_activesite/1'>residues</scene> at the top of the receptor. They then interact with the,<scene name='Sandbox_53/Achr_residues/1'>val 255 and leu 251</scene> residues which define a hydrophobic region through which a dehydrated ion could pass through.
+Atropine first enters the acetylcholine receptor and binds to the <scene name='Sandbox_53/Achr_activesite/1'>residues</scene> at the top of the receptor. They then interact with the,<scene name='Sandbox_53/Achr_residues/1'>val 255 and leu 251</scene> residues which define a hydrophobic region through which a dehydrated ion could pass through. These residues can be seen more clearly through this <scene name='Sandbox_53/Achr_residues2/1'>contacts</scene> representation.
 The interaction of atropine and phospholipase 2A will be discussed in detail later in this article.