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1mry

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{{STRUCTURE_1mry| PDB=1mry | SCENE= }}
{{STRUCTURE_1mry| PDB=1mry | SCENE= }}
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'''crystal structure of an inactive akt2 kinase domain'''
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===crystal structure of an inactive akt2 kinase domain===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12517337 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12517337}}
==Disease==
==Disease==
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[[Category: Tumorigenesis]]
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[[Category: X-ray crystal structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:38:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:11:35 2008''

Revision as of 10:11, 27 July 2008

Image:1mry.png

Template:STRUCTURE 1mry

Contents

crystal structure of an inactive akt2 kinase domain

Template:ABSTRACT PUBMED 12517337

Disease

Known disease associated with this structure: Diabetes mellitus, type II OMIM:[164731]

About this Structure

1MRY 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

Page seeded by OCA on Sun Jul 27 13:11:35 2008

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