1tzd

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(New page: 200px<br /><applet load="1tzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tzd, resolution 2.20&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1tzd.jpg|left|200px]]<br /><applet load="1tzd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tzd, resolution 2.20&Aring;" />
caption="1tzd, resolution 2.20&Aring;" />
'''CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE'''<br />
'''CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE'''<br />
==Overview==
==Overview==
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Soluble inositol polyphosphates are ubiquitous second messengers in, eukaryotes, and their levels are regulated by an array of specialized, kinases. The structure of an archetypal member of this class, inositol, 1,4,5-trisphosphate 3-kinase (IP3K), has been determined at 2.2 angstroms, resolution in complex with magnesium and adenosine diphosphate. IP3K, contains a catalytic domain that is a variant of the protein kinase, superfamily, and a novel four-helix substrate binding domain. The two, domains are in an open conformation with respect to each other, suggesting, that substrate recognition and catalysis by IP3K involves a dynamic, conformational cycle. The unique helical domain of IP3K blocks access to, the active site by membrane-bound phosphoinositides, explaining the, structural basis for soluble inositol polyphosphate specificity.
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Soluble inositol polyphosphates are ubiquitous second messengers in eukaryotes, and their levels are regulated by an array of specialized kinases. The structure of an archetypal member of this class, inositol 1,4,5-trisphosphate 3-kinase (IP3K), has been determined at 2.2 angstroms resolution in complex with magnesium and adenosine diphosphate. IP3K contains a catalytic domain that is a variant of the protein kinase superfamily, and a novel four-helix substrate binding domain. The two domains are in an open conformation with respect to each other, suggesting that substrate recognition and catalysis by IP3K involves a dynamic conformational cycle. The unique helical domain of IP3K blocks access to the active site by membrane-bound phosphoinositides, explaining the structural basis for soluble inositol polyphosphate specificity.
==About this Structure==
==About this Structure==
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1TZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Inositol-trisphosphate_3-kinase Inositol-trisphosphate 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.127 2.7.1.127] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TZD OCA].
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1TZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Inositol-trisphosphate_3-kinase Inositol-trisphosphate 3-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.127 2.7.1.127] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TZD OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
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[[Category: Miller, G.J.]]
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[[Category: Miller, G J.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
[[Category: inositol kinase]]
[[Category: inositol kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:43:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:18:58 2008''

Revision as of 13:19, 21 February 2008


1tzd, resolution 2.20Å

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CRYSTAL STRUCTURE OF THE CATALYTIC CORE OF INOSITOL 1,4,5-TRISPHOSPHATE 3-KINASE

Overview

Soluble inositol polyphosphates are ubiquitous second messengers in eukaryotes, and their levels are regulated by an array of specialized kinases. The structure of an archetypal member of this class, inositol 1,4,5-trisphosphate 3-kinase (IP3K), has been determined at 2.2 angstroms resolution in complex with magnesium and adenosine diphosphate. IP3K contains a catalytic domain that is a variant of the protein kinase superfamily, and a novel four-helix substrate binding domain. The two domains are in an open conformation with respect to each other, suggesting that substrate recognition and catalysis by IP3K involves a dynamic conformational cycle. The unique helical domain of IP3K blocks access to the active site by membrane-bound phosphoinositides, explaining the structural basis for soluble inositol polyphosphate specificity.

About this Structure

1TZD is a Single protein structure of sequence from Rattus norvegicus with and as ligands. Active as Inositol-trisphosphate 3-kinase, with EC number 2.7.1.127 Full crystallographic information is available from OCA.

Reference

Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase., Miller GJ, Hurley JH, Mol Cell. 2004 Sep 10;15(5):703-11. PMID:15350215

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