1gzo

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[[Image:1gzo.jpg|left|200px]]
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{{STRUCTURE_1gzo| PDB=1gzo | SCENE= }}
{{STRUCTURE_1gzo| PDB=1gzo | SCENE= }}
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'''STRUCTURE OF PROTEIN KINASE B UNPHOSPHORYLATED'''
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===STRUCTURE OF PROTEIN KINASE B UNPHOSPHORYLATED===
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==Overview==
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Protein kinase B/Akt plays crucial roles in promoting cell survival and mediating insulin responses. The enzyme is stimulated by phosphorylation at two regulatory sites: Thr 309 of the activation segment and Ser 474 of the hydrophobic motif, a conserved feature of many AGC kinases. Analysis of the crystal structures of the unphosphorylated and Thr 309 phosphorylated states of the PKB kinase domain provides a molecular explanation for regulation by Ser 474 phosphorylation. Activation by Ser 474 phosphorylation occurs via a disorder to order transition of the alphaC helix with concomitant restructuring of the activation segment and reconfiguration of the kinase bilobal structure. These conformational changes are mediated by a phosphorylation-promoted interaction of the hydrophobic motif with a channel on the N-terminal lobe induced by the ordered alphaC helix and are mimicked by peptides corresponding to the hydrophobic motif of PKB and potently by the hydrophobic motif of PRK2.
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The line below this paragraph, {{ABSTRACT_PUBMED_12086620}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 12086620 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12086620}}
==About this Structure==
==About this Structure==
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[[Category: Serine/threonine-protein kinase]]
[[Category: Serine/threonine-protein kinase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:13:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:22:39 2008''

Revision as of 03:22, 1 July 2008

Template:STRUCTURE 1gzo

STRUCTURE OF PROTEIN KINASE B UNPHOSPHORYLATED

Template:ABSTRACT PUBMED 12086620

About this Structure

1GZO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation., Yang J, Cron P, Thompson V, Good VM, Hess D, Hemmings BA, Barford D, Mol Cell. 2002 Jun;9(6):1227-40. PMID:12086620

Page seeded by OCA on Tue Jul 1 06:22:39 2008

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