CRYSTAL-STRUCTURE OF CASEIN KINASE-1, A PHOSPHATE-DIRECTED PROTEIN-KINASE

被引:183
作者
XU, RM
CARMEL, G
SWEET, RM
KURET, J
CHENG, XD
机构
[1] MGC CORP, LAKE BLUFF, IL 60044 USA
[2] COLD SPRING HARBOR LAB, WM KECK STRUCT BIOL LAB, COLD SPRING HARBOR, NY 11724 USA
[3] BROOKHAVEN NATL LAB, DEPT BIOL, UPTON, NY 11973 USA
关键词
CASEIN KINASE-1; NUCLEOTIDE BINDING; PROTEIN KINASE REGULATION; SUBSTRATE SPECIFICITY; STRUCTURAL SIMILARITY;
D O I
10.1002/j.1460-2075.1995.tb07082.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The structure of a truncated variant of casein kinase-1 from Schizosacckaromyces pombe, has been determined in complex with MgATP at 2.0 Angstrom 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.
引用
收藏
页码:1015 / 1023
页数:9
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