1RHW
The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila
Summary for 1RHW
Entry DOI | 10.2210/pdb1rhw/pdb |
NMR Information | BMRB: 6096 |
Descriptor | Dynein light chain 1, cytoplasmic (1 entity in total) |
Functional Keywords | domain swapped, dimer interface, contractile protein |
Biological source | Drosophila melanogaster (fruit fly) |
Cellular location | Cytoplasm, cytoskeleton: Q24117 |
Total number of polymer chains | 1 |
Total formula weight | 10388.85 |
Authors | Makokha, M.,Huang, Y.J.,Montelione, G.,Edison, A.S.,Barbar, E. (deposition date: 2003-11-14, release date: 2004-04-27, Last modification date: 2024-05-22) |
Primary citation | Makokha, M.,Huang, Y.J.,Montelione, G.,Edison, A.S.,Barbar, E. The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila. Protein Sci., 13:727-734, 2004 Cited by PubMed 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 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. PubMed: 14767079DOI: 10.1110/ps.03462204 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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