The three-dimensional structure of human aurora-C kinase predicted by homology modeling

5Citations
Citations of this article
6Readers
Mendeley users who have this article in their library.
Get full text

Abstract

Aurora-C is a key member of a closely related subgroup of serine/threonine kinase that plays an important role in the completion of essential mitotic events. By means of the homology modeling and the known structure of aurora-B, the 3D structure of aurora-C sourced human sapiens is modeled and then refined by using molecular mechanics (MM) optimization and molecular dynamics (MD) simulation. The final refined model is further assessed by Profile-3D and PROCHECK, which shows that this model is reliable. And then, the inhibitors H-89 and H-8 are docked to aurora-C. The docking study shows that Ala149 and Lys134 are important in inhibition as they form hydrogen bonds and have strong nonbonding interaction with H-89. We also suggest that Ile133, His130, and Ile148 are three important residues in binding as they have strong nonbonding interaction with H-89. The high affinity of H-89 compared with H-8 is explained by the much larger value of van der Waals energy with the enzyme. Our results will be helpful for further experimental investigations. © 2007 Elsevier B.V. All rights reserved.

Cite

CITATION STYLE

APA

Han, W. W., Zhou, Y. H., Yao, Y., & Li, Z. S. (2007). The three-dimensional structure of human aurora-C kinase predicted by homology modeling. Journal of Molecular Structure: THEOCHEM, 815(1–3), 87–93. https://doi.org/10.1016/j.theochem.2007.03.020

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free