Protein kinase Spk1

Revision as of 13:30, 14 July 2016 by Michal Harel (talk | contribs)


Function

Protein kinase Spk1 (Rad53) is a serine/threonine protein kinase which phosphorylates proteins. Rad53 controls S-phase checkpoint and G1 and G2 DNA damage checkpoints. Rad53 phosphorylates proteins at serine, threonine and tyrosine residues.

Structural highlights

Rad53 contains phosphothreonine recognition domains: FHA1 at the N-terminal (residues 1-164) which selects for Asp at position +3 relative to phosphothreonine and FHA2 at the C-terminal (residues 573-730) which selects for Ile at position +3 relative to phosphothreonine. Two SCD - SQ/TQ-rich cluster domains – are flanking the kinase domain. The yeast FHA1 domain interacts with peptide containing phosphothreonine[1].

Structure of yeast Rad53 FHA1 domain (grey) complex with phosphothreonine peptide (green) (PDB code 2a0t).

Drag the structure with the mouse to rotate

3D structures of protein kinase Spk13D structures of protein kinase Spk1

Updated on 14-July-2016

ReferencesReferences

  1. Durocher D, Taylor IA, Sarbassova D, Haire LF, Westcott SL, Jackson SP, Smerdon SJ, Yaffe MB. The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol Cell. 2000 Nov;6(5):1169-82. PMID:11106755

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Michal Harel, Alexander Berchansky, Joel L. Sussman