1fj2
From Proteopedia
(New page: 200px<br /> <applet load="1fj2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fj2, resolution 1.5Å" /> '''Crystal structure of...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1FJ2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with BR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.39 3.1.4.39]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJ2 OCA]]. | + | 1FJ2 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with BR as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Alkylglycerophosphoethanolamine_phosphodiesterase Alkylglycerophosphoethanolamine phosphodiesterase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.39 3.1.4.39]]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FJ2 OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A., Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS, Structure. 2000 Nov 15;8(11):1137-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080636 11080636] | Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A., Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS, Structure. 2000 Nov 15;8(11):1137-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11080636 11080636] | ||
| + | [[Category: Alkylglycerophosphoethanolamine phosphodiesterase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine hydrolase]] | [[Category: serine hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:04:11 2007'' |
Revision as of 11:59, 30 October 2007
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Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution
Overview
BACKGROUND: Many proteins undergo posttranslational modifications, involving covalent attachment of lipid groups. Among them is, palmitoylation, a dynamic, reversible process that affects trimeric G, proteins and Ras and constitutes a regulatory mechanism for signal, transduction pathways. Recently, an acylhydrolase previously identified as, lysophospholipase has been shown to function as an acyl protein, thioesterase, which catalyzes depalmitoylation of Galpha proteins as well, as Ras. Its amino acid sequence suggested that the protein is, evolutionarily related to neutral lipases and other thioesterases, but, direct structural information was not available. RESULTS: We have solved, the crystal structure of the human putative Galpha-regulatory protein acyl, thioesterase (hAPT1) with a ... [(full description)]
About this Structure
1FJ2 is a [Single protein] structure of sequence from [Homo sapiens] with BR as [ligand]. Active as [Alkylglycerophosphoethanolamine phosphodiesterase], with EC number [3.1.4.39]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A., Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS, Structure. 2000 Nov 15;8(11):1137-46. PMID:11080636
Page seeded by OCA on Tue Oct 30 14:04:11 2007
