Sandbox c4
From Proteopedia
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<scene name='Sandbox_c4/Phe_and_tyr/1'>(W84 and F330). | <scene name='Sandbox_c4/Phe_and_tyr/1'>(W84 and F330). | ||
</scene><ref>PMID8415649</ref> | </scene><ref>PMID8415649</ref> | ||
| + | The | ||
| + | <scene name='Hemoglobin/Foursubunits/5'>four subunits</scene> of hemoglobin sit roughly at the corners of a tetrahedron, facing each other across a <scene name='Hemoglobin/Cavity/9'>cavity</scene> at the center of the molecule. Each of the subunits <scene name='Hemoglobin/Bbsubunitswithheme/5'>contains a heme</scene> prosthetic group. The <scene name='Hemoglobin/4heme/3'>heme molecules</scene> give hemoglobin its red color. | ||
Current revision
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1ACJ shows the crystal structure of Torpedo californica acetylcholinesterase (TcAChE) complexed with tacrine.
Tacrine is a parasympathomimetic and a centrally acting cholinesterase inhibitor.
It was the first centrally-acting cholinesterase inhibitor approved for the treatment of Alzheimer's disease.
Tacrine’s ring is stacked between the aromatic rings of tryptophan 84 and phenylalanine 330 (W84 and F330).
Harel M, Schalk I, Ehret-Sabatier L, Bouet F, Goeldner M, Hirth C, Axelsen PH, Silman I, Sussman JL. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc Natl Acad Sci U S A. 1993 Oct 1;90(19):9031-5. PMID:8415649 [1] The of hemoglobin sit roughly at the corners of a tetrahedron, facing each other across a at the center of the molecule. Each of the subunits prosthetic group. The give hemoglobin its red color.
