Substrate recognition by casein kinase-II: the role of histidine-160.

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 Lett

journal_title

FEBS letters

authors

Dobrowolska G,Meggio F,Marin O,Lozeman FJ,Li D,Pinna LA,Krebs EG

doi

10.1016/0014-5793(94)01190-7

subject

Has Abstract

pub_date

1994-12-05 00:00:00

pages

237-41

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(94)01190-7

journal_volume

355

pub_type

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