Recently, NEK7 protein, a member of the family of NIMA-related kinases (NEK proteins), has been identified as an NLRP3-binding protein that acts downstream of potassium efflux to regulate NLRP3 assembly and activation .
Nunez, "NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux," Nature, vol.
However, Nek6 and Nek7 are smaller molecules and consist only of a catalytic domain with a moderately short N-terminal expansion.
Crystal structure of APO human Nek7 (PDB ID: 2WQM with 2.10 A resolution) was selected as template, having 82% sequence identity with target.
Accordingly, the crystal structure of Human APO Nek7 is an appreciated template for modeling the 3D structure of Nek6.
The Ramachandran plot residues of Nek6 and 2WQM template (Nek7) were compared for validation (Table 1).
The C-terminal kinase domain of Nek6 protein consists of two important key signatures which includes ATP-binding and Ser/Thr kinases active-site regions, more or less similar to Nek7 protein.
In this study, we have developed a homology model of Nek6 based on known crystal structure of Human APO Nek7 protein, as expected from its sequence similarity.
Caldwell et al., "A mitotic cascade of NIMA family kinases: Nercc1/Nek9 activates the Nek6 and Nek7 kinases," The Journal of Biological Chemistry, vol.