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1mry
From Proteopedia
| 1mry, resolution 2.80Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Gene: | AKT2 (Homo sapiens) | ||||||||
| Activity: | Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 | ||||||||
| Domains: | S_TKc, S_TK_X, S_TKc | ||||||||
| Related: | 1mrv | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
crystal structure of an inactive akt2 kinase domain
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
Disease
Known disease associated with this structure: Diabetes mellitus, type II OMIM:[164731]
About this Structure
1MRY is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Huang X, Begley M, Morgenstern KA, Gu Y, Rose P, Zhao H, Zhu X. Crystal structure of an inactive Akt2 kinase domain. Structure. 2003 Jan;11(1):21-30. PMID:12517337
Page seeded by OCA on Mon Feb 16 11:07:01 2009
