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Table 1 Peptide sequences of domain-phosphopeptide complexes

From: Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics

domain Protein PDB ID Method Phosphopeptide Kd(μM) Ref.
FHA1 Rad53 1G6G X-ray LEV(pT)EADATFAK 0.53 (12)
FHA1 Rad53 1K3Q NMR SLEV(pT)EADATFVQ 0.3 (16)
FHA Dun1 2JQL NMR NI(pT)QP(pT)QQST 0.3-1.2 (35)
FHA Ki67 2AFF NMR KTVD(pS)QGP(pT)PVC(pT)PTFLERRKSQVAELNDDDKDDEIVFKQPISC 0.077 (18)
BRCT BRCA1 1T2V X-ray AAYDI(pS)QVFPFA 0.4 (29)
WW Pin1 1F8A X-ray Y(pS)PT(pS)PS 34 (34)
  1. Residues in the bracket are either pT or pS. The first mutation site is represented by both underline and bold, and the second mutation site is underlined. Secondary structures, α helix and β sheet, are labeled as italic with underline and italic, respectively.