doi: 10.1038/367704a0.
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Affiliations
- PMID: 8107865
- DOI: 10.1038/367704a0
Item in Clipboard
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Nature.
.
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.
Comment in
-
Signal transduction. Hot lips and phosphorylation of protein kinases.Nature. 1994 Feb 24;367(6465):686. doi: 10.1038/367686a0. Nature. 1994. PMID: 8107861 No abstract available.
Similar articles
-
Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5'-triphosphate.Biochemistry. 1996 May 7;35(18):5641-6. doi: 10.1021/bi952723e. Biochemistry. 1996. PMID: 8639522
-
Structure of GSK3beta reveals a primed phosphorylation mechanism.Nat Struct Biol. 2001 Jul;8(7):593-6. doi: 10.1038/89624. Nat Struct Biol. 2001. PMID: 11427888
-
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation.J Mol Biol. 2001 Aug 17;311(3):557-68. doi: 10.1006/jmbi.2001.4890. J Mol Biol. 2001. PMID: 11493009
-
Molecular mechanisms of protein kinase regulation by calcium/calmodulin.Bioorg Med Chem. 2015 Jun 15;23(12):2749-60. doi: 10.1016/j.bmc.2015.04.051. Epub 2015 Apr 24. Bioorg Med Chem. 2015. PMID: 25963826 Review.
-
How MAP kinases are regulated.J Biol Chem. 1995 Jun 23;270(25):14843-6. doi: 10.1074/jbc.270.25.14843. J Biol Chem. 1995. PMID: 7797459 Review. No abstract available.
Cited by
-
Synergistic anticancer effect by targeting CDK2 and EGFR-ERK signaling.J Cell Biol. 2024 Jan 1;223(1):e202203005. doi: 10.1083/jcb.202203005. Epub 2023 Nov 13. J Cell Biol. 2024. PMID: 37955924 Free PMC article.
-
Structural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Sci Rep. 2015 Jun 8;5:11127. doi: 10.1038/srep11127. Sci Rep. 2015. PMID: 26054059 Free PMC article.
-
Co-conserved MAPK features couple D-domain docking groove to distal allosteric sites via the C-terminal flanking tail.PLoS One. 2015 Mar 23;10(3):e0119636. doi: 10.1371/journal.pone.0119636. eCollection 2015. PLoS One. 2015. PMID: 25799139 Free PMC article.
-
Uncoupling p38α nuclear and cytoplasmic functions and identification of two p38α phosphorylation sites on β-catenin: implications for the Wnt signaling pathway in CRC models.Cell Biosci. 2023 Dec 1;13(1):223. doi: 10.1186/s13578-023-01175-4. Cell Biosci. 2023. PMID: 38041178 Free PMC article.
-
Spermiogenesis initiation in Caenorhabditis elegans involves a casein kinase 1 encoded by the spe-6 gene.Genetics. 2002 May;161(1):143-55. doi: 10.1093/genetics/161.1.143. Genetics. 2002. PMID: 12019230 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
Miscellaneous
