Structural highlights
Function
[DYL1_DROME] Acts as a non-catalytic accessory component of a dynein complex (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila.,Makokha M, Huang YJ, Montelione G, Edison AS, Barbar E Protein Sci. 2004 Mar;13(3):727-34. Epub 2004 Feb 6. PMID:14767079[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Makokha M, Huang YJ, Montelione G, Edison AS, Barbar E. The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila. Protein Sci. 2004 Mar;13(3):727-34. Epub 2004 Feb 6. PMID:14767079 doi:10.1110/ps.03462204
