Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

Faming Zhang; Arne Strand; David Robbins; Melanie H. Cobb; Elizabeth J. Goldsmith

doi:10.1038/367704a0

Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

Faming Zhang, Arne Strand, David Robbins, Melanie H. Cobb, Elizabeth J. Goldsmith

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Abstract

The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

Original language	English (US)
Pages (from-to)	704-711
Number of pages	8
Journal	Nature
Volume	367
Issue number	6465
DOIs	https://doi.org/10.1038/367704a0
State	Published - 1994

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title = "Atomic structure of the MAP kinase ERK2 at 2.3 {\AA} resolution",

abstract = "The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.",

author = "Faming Zhang and Arne Strand and David Robbins and Cobb, {Melanie H.} and Goldsmith, {Elizabeth J.}",

year = "1994",

doi = "10.1038/367704a0",

language = "English (US)",

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pages = "704--711",

journal = "Nature",

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T1 - Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

AU - Zhang, Faming

AU - Strand, Arne

AU - Robbins, David

AU - Cobb, Melanie H.

AU - Goldsmith, Elizabeth J.

PY - 1994

Y1 - 1994

N2 - The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

AB - The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes.

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JO - Nature

JF - Nature

IS - 6465

ER -

Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution

Abstract

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