Abstract:
:Casein kinase-II (CK-II) belongs to the protein kinases recognizing serine/threonine in proximity to acidic residues in protein substrates. Crystallography and mutagenesis studies on the cAMP-dependent protein kinase (PKA) disclosed that glutamic acid-170 (E170), is important for interaction of substrates with the enzyme. At a position corresponding to E170 in PKA most Ser/Thr kinases have an aspartic or glutamic acid, while CK-II has a histidine residue (H160). In order to examine the relevance of this substitution for CK-II substrate specificity, a mutant of the catalytic alpha subunit (H160D), in which H160 was changed to aspartic acid, was made. Our results show that H160 is not primarily involved in canonical substrate recognition, but does interact with an acidic residue located at position -2 with respect to the target Ser/Thr.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Dobrowolska G,Meggio F,Marin O,Lozeman FJ,Li D,Pinna LA,Krebs EGdoi
10.1016/0014-5793(94)01190-7subject
Has Abstractpub_date
1994-12-05 00:00:00pages
237-41issue
3eissn
0014-5793issn
1873-3468pii
0014-5793(94)01190-7journal_volume
355pub_type
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