User:Alex Pennington/Sandbox 1: Difference between revisions
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== Structure == | == Structure == | ||
The receptor is a transmembrane pentameric glycoprotein. It has a weight of approximately 300,000 Daltons. It cylindrical in appearance by electron microscopy approximately 16nm in length and 8nm in diameter. The main ion channel is composed of a water pore that runs through the entire length of the protein. If viewed from the synaptic cleft, the protein will look like a pseudo-symmetrical rosette shown in the picture below composed of 10 different aplha and 4 different beta subunits. | |||
[[Image:NR1.jpg]] | |||
=== ACh Binding Sites === | |||
This protein carries anywhere from 2 to 5 [[acetylcholine]] binding sites which are located at the interface between two subunits. Each subunit contributes 3 loops to the binding site. There is also a "principle" side and a "complimentary" side of the subunits. The principle side binding nicotine with a high degree of specificity and the complimentary side binding a wide variety of acetylcholine like molecules. | |||
=== Ion Channel === | |||
The ion channel of the protein is a 20 membered alpha helix bundle. This channel also contributes to the receptor function in three critical aspects: it contains a gating mechanism, it contains a water pore to stabalize ions, and it has a selectivity filter for ion charge. As with most transmembrane alpha helix bundles, it is hydrophobic around the edges to effectively be supported within the membrane, and it is hydrophilic on the inner portion to transport charged ions. | |||
== Function == | == Function == |