1mry: Difference between revisions

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New page: left|200px<br /> <applet load="1mry" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mry, resolution 2.80Å" /> '''crystal structure o...
 
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[[Image:1mry.gif|left|200px]]<br />
[[Image:1mry.gif|left|200px]]<br /><applet load="1mry" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1mry" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1mry, resolution 2.80&Aring;" />
caption="1mry, resolution 2.80&Aring;" />
'''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, 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.
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==
1MRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1MRY OCA].  
1MRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1MRY OCA].  


==Reference==
==Reference==
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[[Category: Gu, Y.]]
[[Category: Gu, Y.]]
[[Category: Huang, X.]]
[[Category: Huang, X.]]
[[Category: Morgenstern, K.A.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:14:27 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:32 2008''