1u6d

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(New page: 200px<br /> <applet load="1u6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u6d, resolution 1.85&Aring;" /> '''Crystal structure o...)
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'''Crystal structure of the Kelch domain of human Keap1'''<br />
'''Crystal structure of the Kelch domain of human Keap1'''<br />
==Overview==
==Overview==
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Keap1 is a substrate adaptor protein for an ubiquitin ligase complex that, targets the Nrf2 transcription factor for degradation. Keap1 binds Nrf2, through its C-terminal Kelch domain, which contains six copies of the, evolutionarily conserved kelch repeat sequence motif. The structure of the, Kelch domain from human Keap1 has been determined by x-ray crystallography, to a resolution of 1.85 A. The Kelch domain forms a 6-bladed, beta-propeller structure, with residues at the C terminus forming the, first strand in the first blade. Key structural roles have been identified, for the highly conserved glycine, tyrosine, and tryptophan residues that, define the kelch repeat sequence motif. In addition, we show that, substitution of a single amino acid located within a loop that extends out, from the bottom of the beta-propeller structure abolishes binding of Nrf2., The structure of the Kelch domain of Keap1 represents a high quality model, for the superfamily of eukaryotic kelch repeat proteins and provides, insight into how disease-causing mutations perturb the structural, integrity of the Kelch domain.
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Keap1 is a substrate adaptor protein for an ubiquitin ligase complex that targets the Nrf2 transcription factor for degradation. Keap1 binds Nrf2 through its C-terminal Kelch domain, which contains six copies of the evolutionarily conserved kelch repeat sequence motif. The structure of the Kelch domain from human Keap1 has been determined by x-ray crystallography to a resolution of 1.85 A. The Kelch domain forms a 6-bladed beta-propeller structure, with residues at the C terminus forming the first strand in the first blade. Key structural roles have been identified for the highly conserved glycine, tyrosine, and tryptophan residues that define the kelch repeat sequence motif. In addition, we show that substitution of a single amino acid located within a loop that extends out from the bottom of the beta-propeller structure abolishes binding of Nrf2. The structure of the Kelch domain of Keap1 represents a high quality model for the superfamily of eukaryotic kelch repeat proteins and provides insight into how disease-causing mutations perturb the structural integrity of the Kelch domain.
==About this Structure==
==About this Structure==
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1U6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U6D OCA].
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1U6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6D OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beamer, L.J.]]
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[[Category: Beamer, L J.]]
[[Category: Hannink, M.]]
[[Category: Hannink, M.]]
[[Category: Li, X.]]
[[Category: Li, X.]]
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[[Category: kelch repeat motif]]
[[Category: kelch repeat motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:32:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:00 2008''

Revision as of 13:21, 21 February 2008


1u6d, resolution 1.85Å

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Crystal structure of the Kelch domain of human Keap1

Overview

Keap1 is a substrate adaptor protein for an ubiquitin ligase complex that targets the Nrf2 transcription factor for degradation. Keap1 binds Nrf2 through its C-terminal Kelch domain, which contains six copies of the evolutionarily conserved kelch repeat sequence motif. The structure of the Kelch domain from human Keap1 has been determined by x-ray crystallography to a resolution of 1.85 A. The Kelch domain forms a 6-bladed beta-propeller structure, with residues at the C terminus forming the first strand in the first blade. Key structural roles have been identified for the highly conserved glycine, tyrosine, and tryptophan residues that define the kelch repeat sequence motif. In addition, we show that substitution of a single amino acid located within a loop that extends out from the bottom of the beta-propeller structure abolishes binding of Nrf2. The structure of the Kelch domain of Keap1 represents a high quality model for the superfamily of eukaryotic kelch repeat proteins and provides insight into how disease-causing mutations perturb the structural integrity of the Kelch domain.

About this Structure

1U6D is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Kelch domain of human Keap1., Li X, Zhang D, Hannink M, Beamer LJ, J Biol Chem. 2004 Dec 24;279(52):54750-8. Epub 2004 Oct 8. PMID:15475350

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