Sandbox11
From Proteopedia
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¤Acetylcholinesterase (AChE) is a tetramer that is connected to the membrane in neuromuscular junctions by a molecule called collagen Q. [[http://www.ncbi.nlm.nih.gov/pubmed/11804574]] | ¤Acetylcholinesterase (AChE) is a tetramer that is connected to the membrane in neuromuscular junctions by a molecule called collagen Q. [[http://www.ncbi.nlm.nih.gov/pubmed/11804574]] | ||
| - | ¤Acetylcholinesterase (AChE) is an monomeric enzyme. Most often, AChE forms a tetramer and binds with a molecule, collagen Q, to connect to the membrane of the neuromuscular junction. [[http://www.ncbi.nlm.nih.gov/pubmed/11804574]]. From the <scene name='Sandbox11/Secondary_structure/3'>secondary structure</scene>, it can be seen that there are 17 <scene name='Sandbox11/Alpha_helix_total/4'>alpha helices</scene> and 14 <scene name='Sandbox11/Beta_strands/3'>beta strands</scene>. There are 2 beta sheets formed from 3 anti-parallel and 11 anti-parallel beta sheets, respectively(maybe highlight with green scene). As the <scene name='Sandbox11/Original_structure/3'>overall tertiary structure</scene> shows, turns, alpha helices, and beta sheets all occupy a portion of the exterior of the protein. The means that the turns must be composed primarily of polar side chains. On the other hand, the alpha helices will be amphipathic with side chain order designated by the helical wheel; the exterior will be filled with polar side chains that can hydrogen bond with water while the inside of the alpha helix will have nonpolar, hydrophobic groups. The beta sheets must also be amphipathic, but the pattern of side chains is alternating polar and nonpolar. In addition, in order to maintain its tertiary structure, the protein has | + | ¤Acetylcholinesterase (AChE) is an monomeric enzyme. Most often, AChE forms a tetramer and binds with a molecule, collagen Q, to connect to the membrane of the neuromuscular junction. [[http://www.ncbi.nlm.nih.gov/pubmed/11804574]]. From the <scene name='Sandbox11/Secondary_structure/3'>secondary structure</scene>, it can be seen that there are 17 <scene name='Sandbox11/Alpha_helix_total/4'>alpha helices</scene> and 14 <scene name='Sandbox11/Beta_strands/3'>beta strands</scene>. There are 2 beta sheets formed from 3 anti-parallel and 11 anti-parallel beta sheets, respectively(maybe highlight with green scene). As the <scene name='Sandbox11/Original_structure/3'>overall tertiary structure</scene> shows, turns, alpha helices, and beta sheets all occupy a portion of the exterior of the protein. The means that the turns must be composed primarily of polar side chains. On the other hand, the alpha helices will be amphipathic with side chain order designated by the helical wheel; the exterior will be filled with polar side chains that can hydrogen bond with water while the inside of the alpha helix will have nonpolar, hydrophobic groups. The beta sheets must also be amphipathic, but the pattern of side chains is alternating polar and nonpolar. In addition, in order to maintain its tertiary structure, the protein has three sulfide bonds, which are covalent bonds that form between cysteine. The <scene name='Sandbox11/Disulfide_bond/2'>disulfide bond</scene> between cysteine 67 and cysteine 94 is 5.03 angstroms. |
| - | + | ||
¤To do: Try to show 4 monomers, better alpha helices, explain polar/nonpolar regions, where binding site is | ¤To do: Try to show 4 monomers, better alpha helices, explain polar/nonpolar regions, where binding site is | ||
| + | <scene name='Sandbox11/Disulfide_bond/2'>TextToBeDisplayed</scene> | ||
<scene name='Sandbox11/Alpha_helix_total/4'>alpha helices</scene> | <scene name='Sandbox11/Alpha_helix_total/4'>alpha helices</scene> | ||
Revision as of 16:01, 21 April 2011
This sandbox is in use until August 1, 2011 for UMass Chemistry 423. Others please do not edit this page. Thanks!
Chem423 Team Projects: Understanding Drug Mechanisms
Andy Kim, Zach Brentzel, Tyler Vlass, Zach Hitzig
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| 1acj, resolution 2.80Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Topic: Acetylcholinesterase bound by Tacrine
Introduction
By Tyler Vlass
Overall structure
By Zach Brentzel
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| 1ea5, resolution 1.80Å () | |||||||||
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| Ligands: | |||||||||
| Activity: | Acetylcholinesterase, with EC number 3.1.1.7 | ||||||||
| Related: | 1amn, 1ax9, 1cfj, 1dx6, 1e3q, 1e66, 1eea, 1eve, 1fss, 1oce, 1qid, 1qie, 1qif, 1qig, 1qih, 1qii, 1qij, 1qik, 1qim, 1qti, 1som, 1vot, 1vxo, 1vxr, 2ace, 2ack, 2dfp, 3ace | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
¤Acetylcholinesterase (AChE) is a tetramer that is connected to the membrane in neuromuscular junctions by a molecule called collagen Q. [[1]]
¤Acetylcholinesterase (AChE) is an monomeric enzyme. Most often, AChE forms a tetramer and binds with a molecule, collagen Q, to connect to the membrane of the neuromuscular junction. [[2]]. From the , it can be seen that there are 17 and 14 . There are 2 beta sheets formed from 3 anti-parallel and 11 anti-parallel beta sheets, respectively(maybe highlight with green scene). As the shows, turns, alpha helices, and beta sheets all occupy a portion of the exterior of the protein. The means that the turns must be composed primarily of polar side chains. On the other hand, the alpha helices will be amphipathic with side chain order designated by the helical wheel; the exterior will be filled with polar side chains that can hydrogen bond with water while the inside of the alpha helix will have nonpolar, hydrophobic groups. The beta sheets must also be amphipathic, but the pattern of side chains is alternating polar and nonpolar. In addition, in order to maintain its tertiary structure, the protein has three sulfide bonds, which are covalent bonds that form between cysteine. The between cysteine 67 and cysteine 94 is 5.03 angstroms. ¤To do: Try to show 4 monomers, better alpha helices, explain polar/nonpolar regions, where binding site is
Binding
By Andy Kim==
Additional Features
By Zach Hitzig
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Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load and display another structure.
Andy Kim, Zach Brentzel, Tyler Vlass, Zach Hitzig-Acetylcholinesterase
