1mrv
From Proteopedia
(New page: 200px<br /> <applet load="1mrv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mrv, resolution 2.80Å" /> '''crystal structure o...) |
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| - | [[Image:1mrv.gif|left|200px]]<br /> | + | [[Image:1mrv.gif|left|200px]]<br /><applet load="1mrv" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1mrv, resolution 2.80Å" /> | caption="1mrv, resolution 2.80Å" /> | ||
'''crystal structure of an inactive Akt2 kinase domain'''<br /> | '''crystal structure of an inactive Akt2 kinase domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Akt/PKB represents a subfamily of three isoforms from the AGC | + | Akt/PKB represents a subfamily of three isoforms from the AGC serine/threonine kinase family. Amplification of Akt activity has been implicated in diseases that involve inappropriate cell survival, including a number of human malignancies. The structure of an inactive and unliganded Akt2 kinase domain reveals several features that distinguish it from other kinases. Most of the alpha helix C is disordered. The activation loop in this structure adopts a conformation that appears to sterically hinder the binding of both ATP and peptide substrate. In addition, an intramolecular disulfide bond is observed between two cysteines in the activation loop. Residues within the linker region between the N- and C-terminal lobes also contribute to the inactive conformation by partially occupying the ATP binding site. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1MRV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gu, Y.]] | [[Category: Gu, Y.]] | ||
[[Category: Huang, X.]] | [[Category: Huang, X.]] | ||
| - | [[Category: Morgenstern, K | + | [[Category: Morgenstern, K A.]] |
[[Category: Rose, P.]] | [[Category: Rose, P.]] | ||
[[Category: Zhao, H.]] | [[Category: Zhao, H.]] | ||
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[[Category: x-ray crystal structure]] | [[Category: x-ray crystal structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:25 2008'' |
Revision as of 11:58, 21 February 2008
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crystal structure of an inactive Akt2 kinase domain
Contents |
Overview
Akt/PKB represents a subfamily of three isoforms from the AGC serine/threonine kinase family. Amplification of Akt activity has been implicated in diseases that involve inappropriate cell survival, including a number of human malignancies. The structure of an inactive and unliganded Akt2 kinase domain reveals several features that distinguish it from other kinases. Most of the alpha helix C is disordered. The activation loop in this structure adopts a conformation that appears to sterically hinder the binding of both ATP and peptide substrate. In addition, an intramolecular disulfide bond is observed between two cysteines in the activation loop. Residues within the linker region between the N- and C-terminal lobes also contribute to the inactive conformation by partially occupying the ATP binding site.
Disease
Known disease associated with this structure: Diabetes mellitus, type II OMIM:[164731]
About this Structure
1MRV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of an inactive Akt2 kinase domain., Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao H, Zhu X, Structure. 2003 Jan;11(1):21-30. PMID:12517337
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