Crystallization and preliminary crystallographic characterization of the PAS domains of EAG and ELK potassium channels.
Per-Arnt-Sim (PAS) domains are ubiquitous in nature; they are approximately 130-amino-acid protein domains that adopt a fairly conserved three-dimensional structure despite their low degree of sequence homology. These domains constitute the N-terminus or, less frequently, the C-terminus of a number of proteins, where they exert regulatory functions. PAS-containing proteins generally display two or more copies of this motif. In this work, the crystallization and preliminary analysis of the PAS domains of two eukaryotic potassium channels from the ether-à-go-go (EAG) family are reported.
Adaixo
Ricardo
R
IBMC-Instituto de Biologia Molecular e Celular, Rua do Campo Alegre 823, Porto 4150-180, Portugal.
Morais-Cabral
João Henrique
JH
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry*; D004331:Drosophila melanogaster / Q000737:chemistry*; D051638:Ether-A-Go-Go Potassium Channels / Q000737:chemistry*; D051379:Mice; D015221:Potassium Channels / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D029721:Drosophila Proteins; C555038:Elk protein, Drosophila; D051638:Ether-A-Go-Go Potassium Channels; D015221:Potassium Channels
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