ArticleBMC structural biology2011
Human Nek6 is a monomeric mostly globular kinase with an unfolded short N-terminal domain.
Article in BMC structural biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Drug Loading and Release: Development and Characterization of a Novel Therapeutic Agent-Nanographene Conjugate.The journal of physical chemistry. B · 2025Article
- NEK kinases in cell cycle regulation, DNA damage response, and cancer progression.Tissue & cell · 2025Review
- Computational insights into NIMA-related kinase 6: unraveling mutational effects on structure and function.Molecular and cellular biochemistry · 2024Article
- NEK Family Review and Correlations with Patient Survival Outcomes in Various Cancer Types.Cancers · 2023Review
- Identification of potent inhibitors of NEK7 protein using a comprehensive computational approach.Scientific reports · 2022Article
- In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022Review
- LncRNA FAM13A-AS1 Promotes Renal Carcinoma Tumorigenesis Through Sponging miR-141-3p to Upregulate NEK6 Expression.Frontiers in molecular biosciences · 2022Article
- Review
- Checking NEKs: Overcoming a Bottleneck in Human Diseases.Molecules (Basel, Switzerland) · 2020Review
- Identification and antitumor activity of a novel inhibitor of the NIMA-related kinase NEK6.Scientific reports · 2018Article
- Nek7 Protects Telomeres from Oxidative DNA Damage by Phosphorylation and Stabilization of TRF1.Molecular cell · 2017Article
- Article
- Kinase inhibitor profile for human nek1, nek6, and nek7 and analysis of the structural basis for inhibitor specificity.Molecules (Basel, Switzerland) · 2015Article
- Characterization of the human NEK7 interactome suggests catalytic and regulatory properties distinct from those of NEK6.Journal of proteome research · 2014Article
- "Stop Ne(c)king around": How interactomics contributes to functionally characterize Nek family kinases.World journal of biological chemistry · 2014Review
- Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.Biochemistry · 2014Article
- Discovery of novel inhibitors for Nek6 protein through homology model assisted structure based virtual screening and molecular docking approaches.TheScientificWorldJournal · 2014Article
- From laptop to benchtop to bedside: structure-based drug design on protein targets.Current pharmaceutical design · 2012Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe NIMA-related kinases (Neks) are widespread among eukaryotes. In mammalians they represent an evolutionarily conserved family of 11 serine/threonine kinases, with 40-45% amino acid sequence identity to the Aspergillus nidulans mitotic regulator NIMA within their catalytic domains. Neks have cell cycle-related functions and were recently described as related to pathologies, particularly cancer, consisting in potential chemotherapeutic targets. Human Nek6, -7 and -9 are involved in the control of mitotic spindle formation, acting together in a mitotic kinase cascade, but their mechanism of regulation remain elusive.
resultsIn this study we performed a biophysical and structural characterization of human Nek6 with the aim of obtaining its low resolution and homology models. SAXS experiments showed that hNek6 is a monomer of a mostly globular, though slightly elongated shape. Comparative molecular modeling together with disorder prediction analysis also revealed a flexible disordered N-terminal domain for hNek6, which we found to be important to mediate interactions with diverse partners. SEC-MALS experiments showed that hNek6 conformation is dependent on its activation/phosphorylation status, a higher phosphorylation degree corresponding to a bigger Stokes radius. Circular dichroism spectroscopy confirmed our in silico predictions of secondary structure content and thermal stability shift assays revealed a slightly higher stability of wild-type hNek6 compared to the activation loop mutant hNek6(S206A).
conclusionsOur data present the first low resolution 3D structure of hNek6 protein in solution. SAXS, comparative modeling and SEC-MALS analysis revealed that hNek6 is a monomeric kinase of slightly elongated shape and a short unfolded N-terminal domain.
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