Abstract
The structure of Drosophila LC8 pH‐induced monomer has been determined by NMR spectroscopy using the program AutoStructure. The structure at pH 3 and 30°C is similar to the individual subunits of mammalian LC8 dimer with the exception that a β strand, which crosses between monomers to form an intersubunit β‐sheet in the dimer, is a flexible loop with turnlike conformations in the monomer. Increased flexibility in the interface region relative to the rest of the protein is confirmed by dynamic measurements based on 15 N relaxation. Comparison of the monomer and dimer structures indicates that LC8 is not a domain swapped dimer.
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CITATION STYLE
Makokha, M., Huang, Y. J., Montelione, G., Edison, A. S., & Barbar, E. (2004). The solution structure of the pH‐induced monomer of dynein light‐chain LC8 from Drosophila. Protein Science, 13(3), 727–734. https://doi.org/10.1110/ps.03462204
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