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<{|style="width:100%; border:1px solid #E1A524; margin-top=1.0em; background: #FFFED1"
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<Structure load='1acj' size='500' frame='true' align='right' caption='Insert caption here' />
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1ACJ shows the crystal structure of Torpedo californica acetylcholinesterase (TcAChE) complexed with tacrine.
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<div style="font-size:175%; padding-top:0.5em; padding-left:30.0px;">Welcome to Proteopedia,</div>
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<div style="border:0px; padding:0px; margin=0px; line-height:2.0em; padding-left:30.0px;">The free, collaborative 3D encyclopedia of proteins & other molecules</div>
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<td align="left" width="50%">[[Proteopedia:About|About]] <font color="blue">•</font> [[Help:Editing|Editing]] <font color="blue">•</font> [[Help:Contents|Help]]</td>
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{{Template:Currently featured article}}
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Tacrine is a parasympathomimetic and a centrally acting cholinesterase inhibitor.
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* [[Hemoglobin]] - the protein in your blood responsible for oxygen transport
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* [[HIV-1 protease]] - a protein made by the HIV virus, crucial for infection
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* [[Lac repressor]] - controls expression of bacterial enzymes involved in lactose metabolism
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It was the first centrally-acting cholinesterase inhibitor approved for the treatment of Alzheimer's disease.
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Tacrine’s ring is stacked between the aromatic rings of tryptophan 84 and phenylalanine 330 (W84 and F330).
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Help expand existing pages like [[1twc]] or [[Prion proteins]]; or [[Help:Editing#How_To_Create_A_New_Page|start a new page]] on your favorite topic. We could use pages on [[DNA]], [[Trypsin]], & [[Myoglobin]], among [[Wanted pages|others]].
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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
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<scene name='Sandbox_c10/Inhibidor/1'>TextToBeDisplayed</scene>
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<ref>PMID8415649</ref> <references/>
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Hemoglobin (Hb), also spelled haemoglobin, (see on the right a three-dimensional representation of a single molecule) is the protein that carries oxygen from the lungs to the tissues where it's needed. The carbon dioxide produced by the consumption of oxygen. In order to function most efficiently, hemoglobin needs to bind to oxygen tightly in the oxygen-rich atmosphere of the lungs and be able to release oxygen rapidly in the relatively oxygen-poor environment of the tissues. It does this in a most elegant and intricately coordinated way.
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** Example: [[1wsu|Elongation factor SelB]], the protein responsible for adding the 21<sup>st</sup> amino acid selenocysteine to a growing protein chain in bacteria, as seen in the PDB's [[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages#Molecule_of_the_Month_.28MotM.29_Series|Molecule of the Month]].
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''Proteopedia - a scientific 'wiki' bridging the rift between 3D structure and function of biomacromolecules'', '''Genome Biology''' 2008, 9:R121 [http://genomebiology.com/2008/9/8/R121 doi:10.1186/gb-2008-9-8-r121]
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__NOEDITSECTION____NOTOC___
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Current revision

Insert caption here

Drag the structure with the mouse to rotate

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]
  1. . PMID:216315890657

Hemoglobin (Hb), also spelled haemoglobin, (see on the right a three-dimensional representation of a single molecule) is the protein that carries oxygen from the lungs to the tissues where it's needed. The carbon dioxide produced by the consumption of oxygen. In order to function most efficiently, hemoglobin needs to bind to oxygen tightly in the oxygen-rich atmosphere of the lungs and be able to release oxygen rapidly in the relatively oxygen-poor environment of the tissues. It does this in a most elegant and intricately coordinated way.

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