Coiled coil in the stalk region of ncd motor protein is nonlocally sustained

Biochemistry
Mie ItoMasaru Tanokura

Abstract

The dimeric structure of kinesin superfamily proteins plays an important role in their motile functions and characteristics. In this study, the coiled-coil-forming property of the stalk region (192-346) of Drosophila ncd, a C-terminal kinesin motor protein, was investigated by synthesizing various peptide fragments. The alpha helicity of a set of 46-residue peptides spanning the stalk region appeared too low to form a coiled-coil dimer, probably because of insufficient continuity of the hydrophobic residues at (a and d) core positions in amphipathic heptad repeats. On the other hand, several peptides with leucine residues introduced at core positions or with extensional sequences with high alpha helicity had an advantage in coiled-coil formation. When we analyzed the thermal and urea-induced unfolding of these dimeric peptides, we identified four domains having a relatively high potential to form coiled coils. Among them, three domains on the C-terminal side of the stalk region, i.e., (252-272), (276-330), and (336-346), were in the same heptad frame, although these potential coiled-coil domains were not self-sustaining individually. This is in sharp contrast to the fragment of human kinesin, (332-369), which has an extremely h...Continue Reading

References

Sep 4, 1997·Nature·U Henningsen, M Schliwa
Jun 29, 2000·Annual Review of Biochemistry·W F DeGradoA Lombardi
Oct 6, 2000·The Journal of Biological Chemistry·F KozielskiM H Koch
Nov 12, 2002·The EMBO Journal·Thomas G WendtAndreas Hoenger

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Citations

May 12, 2010·Journal of Community Health·Siew Man CheongHazizi Abu Saad
Aug 6, 2011·Metabolic Syndrome and Related Disorders·Andrew K G TanSteven T Yen
Sep 6, 2011·Biophysical Journal·Sirish Kaushik Lakkaraju, Wonmuk Hwang
Jul 3, 2017·Journal of Cell Science·Zhen-Yu She, Wan-Xi Yang

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