2uzs

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[[Image:2uzs.jpg|left|200px]]
[[Image:2uzs.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2uzs |SIZE=350|CAPTION= <scene name='initialview01'>2uzs</scene>, resolution 2.46&Aring;
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The line below this paragraph, containing "STRUCTURE_2uzs", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:4ip+Binding+Site+For+Chain+A'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=4IP:INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE'>4IP</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2uzs| PDB=2uzs | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2uzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2uzs OCA], [http://www.ebi.ac.uk/pdbsum/2uzs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2uzs RCSB]</span>
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}}
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'''A TRANSFORMING MUTATION IN THE PLECKSTRIN HOMOLOGY DOMAIN OF AKT1 IN CANCER (AKT1-PH_E17K)'''
'''A TRANSFORMING MUTATION IN THE PLECKSTRIN HOMOLOGY DOMAIN OF AKT1 IN CANCER (AKT1-PH_E17K)'''
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[[Category: Uhlik, M.]]
[[Category: Uhlik, M.]]
[[Category: Zeckner, D J.]]
[[Category: Zeckner, D J.]]
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[[Category: apoptosis]]
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[[Category: Apoptosis]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: carbohydrate metabolism]]
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[[Category: Carbohydrate metabolism]]
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[[Category: glucose metabolism]]
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[[Category: Glucose metabolism]]
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[[Category: glycogen biosynthesis]]
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[[Category: Glycogen biosynthesis]]
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[[Category: glycogen metabolism]]
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[[Category: Glycogen metabolism]]
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[[Category: kinase]]
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[[Category: Kinase]]
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[[Category: nuclear protein]]
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[[Category: Nuclear protein]]
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[[Category: nucleotide-binding]]
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[[Category: Nucleotide-binding]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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[[Category: serine/threonine-protein kinase]]
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[[Category: Serine/threonine-protein kinase]]
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[[Category: sugar transport]]
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[[Category: Sugar transport]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: translation regulation]]
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[[Category: Translation regulation]]
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[[Category: transport]]
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[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:53:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:06:42 2008''
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Revision as of 14:53, 4 May 2008

Image:2uzs.jpg

Template:STRUCTURE 2uzs

A TRANSFORMING MUTATION IN THE PLECKSTRIN HOMOLOGY DOMAIN OF AKT1 IN CANCER (AKT1-PH_E17K)


Overview

Although AKT1 (v-akt murine thymoma viral oncogene homologue 1) kinase is a central member of possibly the most frequently activated proliferation and survival pathway in cancer, mutation of AKT1 has not been widely reported. Here we report the identification of a somatic mutation in human breast, colorectal and ovarian cancers that results in a glutamic acid to lysine substitution at amino acid 17 (E17K) in the lipid-binding pocket of AKT1. Lys 17 alters the electrostatic interactions of the pocket and forms new hydrogen bonds with a phosphoinositide ligand. This mutation activates AKT1 by means of pathological localization to the plasma membrane, stimulates downstream signalling, transforms cells and induces leukaemia in mice. This mechanism indicates a direct role of AKT1 in human cancer, and adds to the known genetic alterations that promote oncogenesis through the phosphatidylinositol-3-OH kinase/AKT pathway. Furthermore, the E17K substitution decreases the sensitivity to an allosteric kinase inhibitor, so this mutation may have important clinical utility for AKT drug development.

About this Structure

2UZS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

A transforming mutation in the pleckstrin homology domain of AKT1 in cancer., Carpten JD, Faber AL, Horn C, Donoho GP, Briggs SL, Robbins CM, Hostetter G, Boguslawski S, Moses TY, Savage S, Uhlik M, Lin A, Du J, Qian YW, Zeckner DJ, Tucker-Kellogg G, Touchman J, Patel K, Mousses S, Bittner M, Schevitz R, Lai MH, Blanchard KL, Thomas JE, Nature. 2007 Jul 26;448(7152):439-44. Epub 2007 Jul 4. PMID:17611497 Page seeded by OCA on Sun May 4 17:53:36 2008

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