We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1unr

From Proteopedia

Revision as of 14:02, 30 October 2007 by OCA (Talk | contribs)
Jump to: navigation, search

1unr, resolution 1.25Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE PH DOMAIN OF PKB ALPHA IN COMPLEX WITH A SULFATE MOLECULE

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

1UNR is a [Single protein] structure of sequence from [Homo sapiens] with SO4 as [ligand]. 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

Page seeded by OCA on Tue Oct 30 16:06:55 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools