NEK7

NEK7

A gene on chromosome 1q31.3 that encodes a NEK serine/threonine protein kinase which plays a key role in cell cycle progression. NEK7 is required for microtubule nucleation activity of the centrosome, cytokinesis and formation of robust mitotic spindles. It interacts with NEK9 and is highly expressed in the lungs, muscle, testes, brain, heart, liver, leukocytes and spleen.
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References in periodicals archive ?
Among these complexes, NLRP3 inflammasome is the best characterized one, which is consisted by NLRP3, apoptosis-associated speck-like protein, serinethreonine kinase NEK7, and procaspase-1 [7].
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 [58].
Nunez, "NEK7 is an essential mediator of NLRP3 activation downstream of potassium efflux," Nature, vol.
Li et al., "NLRP3 activation and mitosis are mutually exclusive events coordinated by NEK7, a new inflammasome component," Nature Immunology, 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.