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1dx4

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(New page: 200px<br /> <applet load="1dx4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dx4, resolution 2.7&Aring;" /> '''ACHE FROM DROSOPHILA...)
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[[Image:1dx4.gif|left|200px]]<br />
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[[Image:1dx4.gif|left|200px]]<br /><applet load="1dx4" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1dx4" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1dx4, resolution 2.7&Aring;" />
caption="1dx4, resolution 2.7&Aring;" />
'''ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE DERIVATIVE 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE'''<br />
'''ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE DERIVATIVE 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE'''<br />
==Overview==
==Overview==
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We have crystallized Drosophila melanogaster acetylcholinesterase and, solved the structure of the native enzyme and of its complexes with two, potent reversible inhibitors, 1,2,3,4-tetrahydro-N-(phenylmethyl)-9-acridinamine and, 1,2,3,4-tetrahydro-N-(3-iodophenyl-methyl)-9-acridinamine--all three at, 2.7 A resolution. The refined structure of D. melanogaster, acetylcholinesterase is similar to that of vertebrate, acetylcholinesterases, for example, human, mouse, and fish, in its overall, fold, charge distribution, and deep active-site gorge, but some of the, surface loops deviate by up to 8 A from their position in the vertebrate, structures, and the C-terminal helix is shifted substantially. The, active-site gorge of the insect enzyme is significantly narrower than that, of Torpedo californica AChE, and its trajectory is shifted several, angstroms. The volume of the lower part of the gorge of the insect enzyme, is approximately 50% of that of the vertebrate enzyme. Upon binding of, either of the two inhibitors, nine aromatic side chains within the, active-site gorge change their conformation so as to interact with the, inhibitors. Some differences in activity and specificity between the, insect and vertebrate enzymes can be explained by comparison of their, three-dimensional structures.
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We have crystallized Drosophila melanogaster acetylcholinesterase and solved the structure of the native enzyme and of its complexes with two potent reversible inhibitors, 1,2,3,4-tetrahydro-N-(phenylmethyl)-9-acridinamine and 1,2,3,4-tetrahydro-N-(3-iodophenyl-methyl)-9-acridinamine--all three at 2.7 A resolution. The refined structure of D. melanogaster acetylcholinesterase is similar to that of vertebrate acetylcholinesterases, for example, human, mouse, and fish, in its overall fold, charge distribution, and deep active-site gorge, but some of the surface loops deviate by up to 8 A from their position in the vertebrate structures, and the C-terminal helix is shifted substantially. The active-site gorge of the insect enzyme is significantly narrower than that of Torpedo californica AChE, and its trajectory is shifted several angstroms. The volume of the lower part of the gorge of the insect enzyme is approximately 50% of that of the vertebrate enzyme. Upon binding of either of the two inhibitors, nine aromatic side chains within the active-site gorge change their conformation so as to interact with the inhibitors. Some differences in activity and specificity between the insect and vertebrate enzymes can be explained by comparison of their three-dimensional structures.
==About this Structure==
==About this Structure==
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1DX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with NAG, SO4 and 760 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DX4 OCA].
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1DX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=760:'>760</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DX4 OCA].
==Reference==
==Reference==
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[[Category: Harel, M.]]
[[Category: Harel, M.]]
[[Category: Silman, I.]]
[[Category: Silman, I.]]
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[[Category: Sussman, J.L.]]
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[[Category: Sussman, J L.]]
[[Category: 760]]
[[Category: 760]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: synapse]]
[[Category: synapse]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 12:39:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:24 2008''

Revision as of 10:21, 21 February 2008

Image:1dx4.gif

1dx4, resolution 2.7Å

Drag the structure with the mouse to rotate

ACHE FROM DROSOPHILA MELANOGASTER COMPLEX WITH TACRINE DERIVATIVE 9-(3-PHENYLMETHYLAMINO)-1,2,3,4-TETRAHYDROACRIDINE

Overview

We have crystallized Drosophila melanogaster acetylcholinesterase and solved the structure of the native enzyme and of its complexes with two potent reversible inhibitors, 1,2,3,4-tetrahydro-N-(phenylmethyl)-9-acridinamine and 1,2,3,4-tetrahydro-N-(3-iodophenyl-methyl)-9-acridinamine--all three at 2.7 A resolution. The refined structure of D. melanogaster acetylcholinesterase is similar to that of vertebrate acetylcholinesterases, for example, human, mouse, and fish, in its overall fold, charge distribution, and deep active-site gorge, but some of the surface loops deviate by up to 8 A from their position in the vertebrate structures, and the C-terminal helix is shifted substantially. The active-site gorge of the insect enzyme is significantly narrower than that of Torpedo californica AChE, and its trajectory is shifted several angstroms. The volume of the lower part of the gorge of the insect enzyme is approximately 50% of that of the vertebrate enzyme. Upon binding of either of the two inhibitors, nine aromatic side chains within the active-site gorge change their conformation so as to interact with the inhibitors. Some differences in activity and specificity between the insect and vertebrate enzymes can be explained by comparison of their three-dimensional structures.

About this Structure

1DX4 is a Single protein structure of sequence from Drosophila melanogaster with , and as ligands. Active as Acetylcholinesterase, with EC number 3.1.1.7 Full crystallographic information is available from OCA.

Reference

Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors., Harel M, Kryger G, Rosenberry TL, Mallender WD, Lewis T, Fletcher RJ, Guss JM, Silman I, Sussman JL, Protein Sci. 2000 Jun;9(6):1063-72. PMID:10892800

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