1G6G

X-RAY STRUCTURE OF THE N-TERMINAL FHA DOMAIN FROM S. CEREVISIAE RAD53P IN COMPLEX WITH A PHOSPHOTHREONINE PEPTIDE AT 1.6 A RESOLUTION

Summary for 1G6G

• Entry DOI: 10.2210/pdb1g6g/pdb
• Descriptor: PROTEIN KINASE RAD53, SER-LEU-GLU-VAL-TPO-GLU-ALA-ASPALA-THR-PHE-ALA-LYS (3 entities in total)
• Functional Keywords: beta-sandwich, phosphopeptide complex, cell cycle
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P22216
• Total number of polymer chains: 4
• Total formula weight: 31183.20

Authors

Durocher, D.,Taylor, I.A. (deposition date: 2000-11-06, release date: 2000-12-13, Last modification date: 2024-10-30)

Primary citation

Durocher, D.,Taylor, I.A.,Sarbassova, D.,Haire, L.F.,Westcott, S.L.,Jackson, S.P.,Smerdon, S.J.,Yaffe, M.B.
The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.
Mol.Cell, 6:1169-1182, 2000

PubMed Abstract: Forkhead-associated (FHA) domains are a class of ubiquitous signaling modules that appear to function through interactions with phosphorylated target molecules. We have used oriented peptide library screening to determine the optimal phosphopeptide binding motifs recognized by several FHA domains, including those within a number of DNA damage checkpoint kinases, and determined the X-ray structure of Rad53p-FHA1, in complex with a phospho-threonine peptide, at 1.6 A resolution. The structure reveals a striking similarity to the MH2 domains of Smad tumor suppressor proteins and reveals a mode of peptide binding that differs from SH2, 14-3-3, or PTB domain complexes. These results have important implications for DNA damage signaling and CHK2-dependent tumor suppression, and they indicate that FHA domains play important and unsuspected roles in S/T kinase signaling mechanisms in prokaryotes and eukaryotes.

PubMed: 11106755
DOI: 10.1016/S1097-2765(00)00114-3

Experimental method

X-RAY DIFFRACTION (1.6 Å)