|Protein Science (2004) 13(3):727-34|
|Northeast Structural Genomics Consortium|
(click to unfold)
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 degrees C 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 (15)N relaxation. Comparison of the monomer and dimer structures indicates that LC8 is not a domain swapped dimer.
|chemistry genetics |
|Drosophila Proteins Models, Molecular Recombinant Proteins Protein Structure, Tertiary Dyneins Protein Conformation Isotope Labeling Animals Protein Subunits Protein Structure, Secondary Carrier Proteins Drosophila Nuclear Magnetic Resonance, Biomolecular Structural Homology, Protein Hydrogen-Ion Concentration |
|29 (Last update: 05/27/2017 12:12:56pm)|
|Protein Sci. 2004 Mar;13(3):727-34. Epub 2004 Feb 6.|