Structural highlights
Function
[CKI1_SCHPO] Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a truncated variant of casein kinase-1 from Schizosaccharomyces pombe, has been determined in complex with MgATP at 2.0 A resolution. The model resembles the 'closed', ATP-bound conformations of the cyclin-dependent kinase 2 and the cAMP-dependent protein kinase, with clear differences in the structure of surface loops that impart unique features to casein kinase-1. The structure is of unphosphorylated, active conformation of casein kinase-1 and the peptide-binding site is fully accessible to substrate.
Crystal structure of casein kinase-1, a phosphate-directed protein kinase.,Xu RM, Carmel G, Sweet RM, Kuret J, Cheng X EMBO J. 1995 Mar 1;14(5):1015-23. PMID:7889932[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xu RM, Carmel G, Sweet RM, Kuret J, Cheng X. Crystal structure of casein kinase-1, a phosphate-directed protein kinase. EMBO J. 1995 Mar 1;14(5):1015-23. PMID:7889932
