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PDBsum entry 2zoq
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References listed in PDB file
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Key reference
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Title
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Crystal structure of human mono-Phosphorylated erk1 at tyr204.
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Authors
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T.Kinoshita,
I.Yoshida,
S.Nakae,
K.Okita,
M.Gouda,
M.Matsubara,
K.Yokota,
H.Ishiguro,
T.Tada.
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Ref.
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Biochem Biophys Res Commun, 2008,
377,
1123-1127.
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PubMed id
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Abstract
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Extracellular signal-regulated kinase (ERK) is a member of the MAP kinase
family, and can regulate several cellular responses. The isoforms ERK1 and ERK2
have markedly similar amino acid sequences, but exhibit distinctive
physiological functions. As well as ERK2, ERK1 was auto- and mono-phosphorylated
at Tyr204 in the activation loop during Escherichia coli production, resulting
in basal level activity, approximately 500-fold less compared with fully-active
ERK1 dual-phosphorylated at Thr202 and Tyr204. Crystal structure demonstrated
that the mono-phosphorylated ERK1 kinase possessed a novel conformation
distinguishable from the un-phosphorylated (inactive) and the
dual-phosphorylated (full-active) forms. The characteristic structural features
in both the C-helix and the activation loop likely contribute to the basal
activity of the mono-phosphorylated ERK1. The structural dissection of ERK1
compared to ERK2 suggests that the structural differences in the D-motif binding
site and in the backside binding site are putative targets for development of
selective ERK1/ERK2 inhibitors.
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