Substrate recognition by casein kinase‐II: The role of histidine‐160

FEBS Letters

Dobrowolska, Grazyna¹  Li, Dongxia¹  Lozeman, Fred J.¹  Pinna, Lorenzo A.²  Marin, Oriano²  Meggio, Flavio²  Krebs, Edwin G.¹ 

[1] University of Washington, Department of Pharmacology, SL-15, Seattle, WA 98195, USA;Università di Padova, Dipartimento di Chimica Biologica, CRIBI and Centro per lo Studio della Fisiologia Mitocondriale, via Trieste 75, 35121 Padova, Italy

关键词: Casein kinase-II;    α subunit;    Specificity;    Phosphorylation;    Peptide;   

DOI  :  10.1016/0014-5793(94)01190-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 α 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.

【 授权许可】

Unknown