1zgk

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[[Image:1zgk.gif|left|200px]]
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{{Seed}}
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[[Image:1zgk.png|left|200px]]
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{{STRUCTURE_1zgk| PDB=1zgk | SCENE= }}
{{STRUCTURE_1zgk| PDB=1zgk | SCENE= }}
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'''1.35 angstrom structure of the Kelch domain of Keap1'''
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===1.35 angstrom structure of the Kelch domain of Keap1===
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==Overview==
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The Kelch repeat is a common sequence motif in eukaryotic genomes and is approximately 50 amino acids in length. The structure of the Kelch domain of the human Keap1 protein has previously been determined at 1.85 Angstrom, showing that each Kelch repeat forms one blade of a six-bladed beta-propeller. Here, use of 1.35 Angstrom SAD data for de novo structure determination of the Kelch domain and for refinement at atomic resolution is described. The high quality and resolution of the diffraction data and phase information allows a detailed analysis of the role of solvent in the structure of the Kelch repeat. Ten structurally conserved water molecules are identified in each blade of the Kelch beta-propeller. These appear to play distinct structural roles that include lining the central channel of the propeller, interacting with residues in loops between strands of the blade and making contacts with conserved residues in the Kelch repeat. Furthermore, we identify a conserved C-H...pi hydrogen bond between two key residues in the consensus Kelch repeat. This analysis extends our understanding of the structural roles of conserved residues in the Kelch repeat and highlights the potential role of solvent in maintaining the fold of this common eukaryotic structural motif.
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The line below this paragraph, {{ABSTRACT_PUBMED_16204884}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 16204884 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16204884}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1., Beamer LJ, Li X, Bottoms CA, Hannink M, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1335-42. Epub 2005, Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16204884 16204884]
Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1., Beamer LJ, Li X, Bottoms CA, Hannink M, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1335-42. Epub 2005, Sep 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16204884 16204884]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15475350 15475350]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beta-propeller]]
[[Category: Beta-propeller]]
[[Category: Kelch repeat motif]]
[[Category: Kelch repeat motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:35:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:00:51 2008''

Revision as of 07:00, 29 July 2008

Image:1zgk.png

Template:STRUCTURE 1zgk

1.35 angstrom structure of the Kelch domain of Keap1

Template:ABSTRACT PUBMED 16204884

About this Structure

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

Reference

Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1., Beamer LJ, Li X, Bottoms CA, Hannink M, Acta Crystallogr D Biol Crystallogr. 2005 Oct;61(Pt 10):1335-42. Epub 2005, Sep 28. PMID:16204884

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

Page seeded by OCA on Tue Jul 29 10:00:51 2008

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