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1unq

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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:06:44 2007''
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Revision as of 14:02, 30 October 2007

Image:1unq.gif

1unq, resolution 0.98Å

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HIGH RESOLUTION CRYSTAL STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B/AKT BOUND TO INS (1,3,4,5)-TETRAKISPHOPHATE

Overview

Protein kinase B (PKB/Akt) is a key regulator of cell growth, proliferation and metabolism. It possesses an N-terminal pleckstrin, homology (PH) domain that interacts with equal affinity with the second, messengers PtdIns(3,4,5)P3 and PtdIns(3,4)P2, generated through insulin, and growth factor-mediated activation of phosphoinositide 3-kinase (PI3K)., The binding of PKB to PtdIns(3,4,5)P3/PtdIns(3,4)P2 recruits PKB from the, cytosol to the plasma membrane and is also thought to induce a, conformational change that converts PKB into a substrate that can be, activated by the phosphoinositide-dependent kinase 1 (PDK1). In this study, we describe two high-resolution crystal structures of the PH domain of, PKBalpha in a noncomplexed form and compare this to a new atomic, resolution (0.98 A, ... [(full description)]

About this Structure

1UNQ is a [Single protein] structure of sequence from [Homo sapiens] with ACE and 4IP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change., Milburn CC, Deak M, Kelly SM, Price NC, Alessi DR, Van Aalten DM, Biochem J. 2003 Nov 1;375(Pt 3):531-8. PMID:12964941

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