期刊
PROTEIN SCIENCE
卷 13, 期 3, 页码 727-734出版社
WILEY
DOI: 10.1110/ps.03462204
关键词
domain swapping; protein structure; dimerization; dynein light chain; pH-induced dissociation
The structure of Drosophila LC8 pH-induced monomer has been determined by NMR spectroscopy using , the program AutoStructure. The structure at pH 3 and 30degreesC is similar to the individual subunits of mammalian LC8 dimer with the exception that a beta strand, which crosses between monomers to form an intersubunit beta-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 N-15 relaxation. Comparison of the monomer and dimer structures indicates that LC8 is not a domain swapped dimer.
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