Sandbox 1b41: Difference between revisions
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{{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. | ||
It has an ellipsoidal shape with dimensions ~ 4,5nm x 6nm x 6,5nm. It consists of 12-stranded, central mixed <scene name='Sandbox_1b41/B_sheets/1'>β-sheet</scene> surrounded by 14 <scene name='Sandbox_1b41/A_helix/1'>α helices</scene>. | It has an ellipsoidal shape with dimensions ~ 4,5nm x 6nm x 6,5nm. This protein is composed of 531 residues. It consists of 12-stranded, central mixed <scene name='Sandbox_1b41/B_sheets/1'>β-sheet</scene> surrounded by 14 <scene name='Sandbox_1b41/A_helix/1'>α helices</scene>. | ||
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 "tryptophan amphiphilic tetramerization" domain (WAT). There is also a monomeric form which is soluble in the blood. | 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 "tryptophan amphiphilic tetramerization" domain (WAT). There is also a monomeric form which is soluble in the blood. | ||
