1i09

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(New page: 200px<br /> <applet load="1i09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i09, resolution 2.7&Aring;" /> '''STRUCTURE OF GLYCOGE...)
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<applet load="1i09" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1i09, resolution 2.7&Aring;" />
caption="1i09, resolution 2.7&Aring;" />
'''STRUCTURE OF GLYCOGEN SYNTHASE KINASE-3 (GSK3B)'''<br />
'''STRUCTURE OF GLYCOGEN SYNTHASE KINASE-3 (GSK3B)'''<br />
==Overview==
==Overview==
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GSK3beta was identified as the kinase that phosphorylates glycogen, synthase but is now known to be involved in multiple signaling pathways., GSK3beta prefers prior phosphorylation of its substrates. We present the, structure of unphosphorylated GSK3beta at 2.7 A. The orientation of the, two domains and positioning of the activation loop of GSK3beta are similar, to those observed in activated kinases. A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies the same position as the phosphate group of, the phosphothreonine in activated p38gamma, CDK2 or ERK2. A loop from a, neighboring molecule in the crystal occupies a portion of the substrate, binding groove. The structure explains the unique primed phosphorylation, mechanism of GSK3beta and how GSK3beta relies on a phosphoserine in the, substrate for the alignment of the beta- and alpha-helical domains.
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GSK3beta was identified as the kinase that phosphorylates glycogen synthase but is now known to be involved in multiple signaling pathways. GSK3beta prefers prior phosphorylation of its substrates. We present the structure of unphosphorylated GSK3beta at 2.7 A. The orientation of the two domains and positioning of the activation loop of GSK3beta are similar to those observed in activated kinases. A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies the same position as the phosphate group of the phosphothreonine in activated p38gamma, CDK2 or ERK2. A loop from a neighboring molecule in the crystal occupies a portion of the substrate binding groove. The structure explains the unique primed phosphorylation mechanism of GSK3beta and how GSK3beta relies on a phosphoserine in the substrate for the alignment of the beta- and alpha-helical domains.
==About this Structure==
==About this Structure==
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1I09 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I09 OCA].
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1I09 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 <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I09 OCA].
==Reference==
==Reference==
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[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Coll, J.T.]]
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[[Category: Coll, J T.]]
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[[Category: Haar, E.Ter.]]
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[[Category: Haar, E Ter.]]
[[Category: Jain, J.]]
[[Category: Jain, J.]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: kinase]]
[[Category: kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:24:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:37 2008''

Revision as of 11:06, 21 February 2008


1i09, resolution 2.7Å

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STRUCTURE OF GLYCOGEN SYNTHASE KINASE-3 (GSK3B)

Overview

GSK3beta was identified as the kinase that phosphorylates glycogen synthase but is now known to be involved in multiple signaling pathways. GSK3beta prefers prior phosphorylation of its substrates. We present the structure of unphosphorylated GSK3beta at 2.7 A. The orientation of the two domains and positioning of the activation loop of GSK3beta are similar to those observed in activated kinases. A phosphate ion held by Arg 96, Arg 180 and Lys 205 occupies the same position as the phosphate group of the phosphothreonine in activated p38gamma, CDK2 or ERK2. A loop from a neighboring molecule in the crystal occupies a portion of the substrate binding groove. The structure explains the unique primed phosphorylation mechanism of GSK3beta and how GSK3beta relies on a phosphoserine in the substrate for the alignment of the beta- and alpha-helical domains.

About this Structure

1I09 is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

Reference

Structure of GSK3beta reveals a primed phosphorylation mechanism., ter Haar E, Coll JT, Austen DA, Hsiao HM, Swenson L, Jain J, Nat Struct Biol. 2001 Jul;8(7):593-6. PMID:11427888

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