Sandbox 1b41: Difference between revisions
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==Human Acetylcholinesterase (1b41)== | ==Human Acetylcholinesterase (1b41)== | ||
{{STRUCTURE_1b41 | PDB=1b41 | SCENE= }} | {{STRUCTURE_1b41 | PDB=1b41 | SCENE= }} | ||
The human acetylcholinesterase (AChE) is an enzyme which hydrolyses the neurotransmitter Acethylcholin (ACh) in the neuromuscular junctions and in other cholinergic synapses to terminate the neuronal signal. | The human acetylcholinesterase (AChE) is an enzyme which hydrolyses the neurotransmitter Acethylcholin (ACh) in the neuromuscular junctions and in other cholinergic synapses to terminate the neuronal signal. | ||
In the physiological conditions, AChE exists as tetramers associated with either collagen-like Q subunit (ColQ) or proline-rich membrane-anchoring protein (PRiMA). There is also a monomeric form which is soluble in the blood. | It has an ellipsoidal shape with dimensions ~ 4,5nm x 6nm x 6,5nm. It consists of 12-stranded, central mixed β-sheet surrounded by 14 ά helices. | ||
In the physiological conditions, AChE exists as tetramers associated with either collagen-like Q subunit (ColQ) or proline-rich membrane-anchoring protein (PRiMA). The AChE is linked with these anchoring molecules by a "the tryptophan amphiphilic tetramerization" domain (WAT). There is also a monomeric form which is soluble in the blood. | |||
[[Image:Acetylcholine.jpg]] | [[Image:Acetylcholine.jpg]] | ||
==The Active site gorge of AChE== | |||
The active site of AChE involved two sites: the peripheral site and the catalytic site (Figure ). | |||
The peripheral site is a transitional binding site of the substrate. It provides three conserved aromatic residues (Tyr, Trp, Tyr) that guide the ligands (ACh or other agonists) by setting an array of low-affinity binding sites. | |||
