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TitleSolution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53.
Journal, issue, pagesJ. Mol. Biol., Vol. 314, Page 563-575, Year 2001
Publish dateOct 3, 2001 (structure data deposition date)
AuthorsYuan, C. / Yongkiettrakul, S. / Byeon, I.J. / Zhou, S. / Tsai, M.D.
External linksJ. Mol. Biol. / PubMed:11846567
MethodsNMR (solution)
Structure data

PDB-1j4o:
REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53
Method: SOLUTION NMR

PDB-1j4p:
NMR STRUCTURE OF THE FHA1 DOMAIN OF RAD53 IN COMPLEX WITH A RAD9-DERIVED PHOSPHOTHREONINE (AT T155) PEPTIDE
Method: SOLUTION NMR

PDB-1j4q:
NMR STRUCTURE OF THE FHA1 DOMAIN OF RAD53 IN COMPLEX WITH A RAD9-DERIVED PHOSPHOTHREONINE (AT T192) PEPTIDE
Method: SOLUTION NMR

PDB-1k3j:
Refined NMR Structure of the FHA1 Domain of Yeast Rad53
Method: SOLUTION NMR

PDB-1k3n:
NMR Structure of the FHA1 Domain of Rad53 in Complex with a Rad9-derived Phosphothreonine (at T155) Peptide
Method: SOLUTION NMR

PDB-1k3q:
NMR structure of the FHA1 Domain of Rad53 in Complex with a Rad9-derived Phosphothreonine (at T192) Peptide
Method: SOLUTION NMR

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSFERASE / FHA DOMAIN / RAD53 / RAD9 / PHOSPHOTHREONINE / PHOSPHOPROTEIN / TRANSFERASE/CELL CYCLE / TRANSFERASE-CELL CYCLE COMPLEX

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