1DMZ

A REFINED NMR STRUCTURE OF A NEW PHOPHOPEPTIDE-BINDING DOMAIN CONTAINING THE FHA2 OF RAD53

Summary for 1DMZ

• Entry DOI: 10.2210/pdb1dmz/pdb
• Related: 1QU5
• Descriptor: PROTEIN (PROTEIN KINASE SPK1) (1 entity in total)
• Functional Keywords: beta-sandwich, antiparallel beta-sheets, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus: P22216
• Total number of polymer chains: 1
• Total formula weight: 18148.76

Authors

Byeon, I.-J.L.,Liao, H.,Tsai, M.-D. (deposition date: 1999-12-15, release date: 2000-01-06, Last modification date: 2024-05-22)

Primary citation

Liao, H.,Byeon, I.J.,Tsai, M.D.
Structure and Function of a New Phosphopeptide-Binding Domain Containing the Fha2 of Rad53
J.Mol.Biol., 294:1041-1049, 1999

PubMed Abstract: The forkhead-associated (FHA) domain is a 55-75 amino acid residue module found in >20 proteins from yeast to human. It has been suggested to participate in signal transduction pathways, perhaps via protein-protein interactions involving recognition of phosphopeptides. Neither the structure nor the ligand of FHA is known. Yeast Rad53, a checkpoint protein involved in DNA damage response, contains two FHA domains, FHA1 (residues 66-116) and FHA2 (residues 601-664), the second of which recognizes phosphorylated Rad9. We herein report the solution structure of an "FHA2-containing domain" of Rad53 (residues 573-730). The structure consists of a beta-sandwich containing two antiparallel beta-sheets and a short, C-terminal alpha-helix. Binding experiments suggested that the FHA2-containing domain specifically recognizes pTyr and a pTyr-containing peptide from Rad9, and that the binding site involves residues highly conserved across FHA domains. The results, along with other recent reports, suggest that FHA domains could have pTyr and pSer/Thr dual specificity.

PubMed: 10588905
DOI: 10.1006/jmbi.1999.3313

Experimental method

SOLUTION NMR