1MRY
crystal structure of an inactive akt2 kinase domain
Summary for 1MRY
| Entry DOI | 10.2210/pdb1mry/pdb |
| Related | 1MRV |
| Descriptor | RAC-beta serine/threonine kinase (2 entities in total) |
| Functional Keywords | agc serine threonine kinase, akt pkb kinase domain, tumorigenesis, x-ray crystal structure, signal transduction, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 39313.01 |
| Authors | Huang, X.,Begley, M.,Morgenstern, K.A.,Gu, Y.,Rose, P.,Zhao, H.,Zhu, X. (deposition date: 2002-09-18, release date: 2003-09-23, Last modification date: 2024-11-13) |
| Primary citation | Huang, X.,Begley, M.,Morgenstern, K.A.,Gu, Y.,Rose, P.,Zhao, H.,Zhu, X. Crystal structure of an inactive akt2 kinase domain Structure, 11:21-30, 2003 Cited by PubMed Abstract: 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. PubMed: 12517337DOI: 10.1016/S0969-2126(02)00937-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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