Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1

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...

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Veröffentlicht in:	Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2005-10, Vol.61 (Pt 10), p.1335-1342
Hauptverfasser:	Beamer, Lesa J, Li, Xuchu, Bottoms, Christopher A, Hannink, Mark
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Motifs Animals Conserved Sequence Crystallography, X-Ray Humans Hydrogen - chemistry Intracellular Signaling Peptides and Proteins Kelch-Like ECH-Associated Protein 1 Models, Molecular Molecular Conformation Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Water - chemistry
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