1x2j: Difference between revisions

Revision as of 22:32, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1x2j.png

Template:STRUCTURE 1x2j

Structural basis for the defects of human lung cancer somatic mutations in the repression activity of Keap1 on Nrf2Structural basis for the defects of human lung cancer somatic mutations in the repression activity of Keap1 on Nrf2

Template:ABSTRACT PUBMED 16507366

About this StructureAbout this Structure

1X2J is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for defects of Keap1 activity provoked by its point mutations in lung cancer., Padmanabhan B, Tong KI, Ohta T, Nakamura Y, Scharlock M, Ohtsuji M, Kang MI, Kobayashi A, Yokoyama S, Yamamoto M, Mol Cell. 2006 Mar 3;21(5):689-700. PMID:16507366

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Structural basis for the defects of human lung cancer somatic mutations in the repression activity of Keap1 on Nrf2'''
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-==Overview==
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-Nrf2 regulates the cellular oxidative stress response, whereas Keap1 represses Nrf2 through its molecular interaction. To elucidate the molecular mechanism of the Keap1 and Nrf2 interaction, we resolved the six-bladed beta propeller crystal structure of the Kelch/DGR and CTR domains of mouse Keap1 and revealed that extensive inter- and intrablade hydrogen bonds maintain the structural integrity and proper association of Keap1 with Nrf2. A peptide containing the ETGE motif of Nrf2 binds the beta propeller of Keap1 at the entrance of the central cavity on the bottom side via electrostatic interactions with conserved arginine residues. We found a somatic mutation and a gene variation in human lung cancer cells that change glycine to cysteine in the DGR domain, introducing local conformational changes that reduce Keap1's affinity for Nrf2. These results provide a structural basis for the loss of Keap1 function and gain of Nrf2 function.
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