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1RHW

The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila

Summary for 1RHW
Entry DOI10.2210/pdb1rhw/pdb
NMR InformationBMRB: 6096
DescriptorDynein light chain 1, cytoplasmic (1 entity in total)
Functional Keywordsdomain swapped, dimer interface, contractile protein
Biological sourceDrosophila melanogaster (fruit fly)
Cellular locationCytoplasm, cytoskeleton: Q24117
Total number of polymer chains1
Total formula weight10388.85
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 citationMakokha, 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: 14767079
DOI: 10.1110/ps.03462204
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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