Bacterial Production of CDKL5 Catalytic Domain: Insights in Aggregation, Internal Translation and Phosphorylation Patterns.
CDKL5
TXY motif
aggregation
chaperones
kinase
phosphorylation
solubility tag
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
15 Aug 2024
15 Aug 2024
Historique:
received:
19
06
2024
revised:
09
08
2024
accepted:
13
08
2024
medline:
31
8
2024
pubmed:
31
8
2024
entrez:
29
8
2024
Statut:
epublish
Résumé
Cyclin-dependent kinase-like 5 (CDKL5) is a serine/threonine protein kinase involved in human brain development and functioning. Mutations in CDKL5, especially in its catalytic domain, cause a severe developmental condition named CDKL5 deficiency disorder. Nevertheless, molecular studies investigating the structural consequences of such mutations are still missing. The CDKL5 catalytic domain harbors different sites of post-translational modification, such as phosphorylations, but their role in catalytic activity, protein folding, and stability has not been entirely investigated. With this work, we describe the expression pattern of the CDKL5 catalytic domain in
Identifiants
pubmed: 39201578
pii: ijms25168891
doi: 10.3390/ijms25168891
pii:
doi:
Substances chimiques
Protein Serine-Threonine Kinases
EC 2.7.11.1
CDKL5 protein, human
EC 2.7.11.22
Protein Aggregates
0
Recombinant Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : the University of Pennsylvania Orphan Disease Center CDKL5-20-101-08
ID : CDKL5-20-101-08