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

Table 1 Peptide sequences of domain-phosphopeptide complexes

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)

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.

ISSN: 2046-1682