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2jv3

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|ACTIVITY=
|ACTIVITY=
|GENE= Ets1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
|GENE= Ets1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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|DOMAIN=
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|RELATEDENTRY=[[1bqv|1BQV]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jv3 OCA], [http://www.ebi.ac.uk/pdbsum/2jv3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jv3 RCSB]</span>
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[[Category: transcription factor]]
[[Category: transcription factor]]
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Revision as of 01:01, 31 March 2008


PDB ID 2jv3

Drag the structure with the mouse to rotate
Gene: Ets1 (Mus musculus)
Related: 1BQV


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Ets-1 PNT domain (29-138) NMR structure ensemble


Overview

The Pointed (PNT) domain and an adjacent mitogen-activated protein (MAP) kinase phosphorylation site are defined by sequence conservation among a subset of ets transcription factors and are implicated in two regulatory strategies, protein interactions and posttranslational modifications, respectively. By using NMR, we have determined the structure of a 110-residue fragment of murine Ets-1 that includes the PNT domain and MAP kinase site. The Ets-1 PNT domain forms a monomeric five-helix bundle. The architecture is distinct from that of any known DNA- or protein-binding module, including the helix-loop-helix fold proposed for the PNT domain of the ets protein TEL. The MAP kinase site is in a highly flexible region of both the unphosphorylated and phosphorylated forms of the Ets-1 fragment. Phosphorylation alters neither the structure nor monomeric state of the PNT domain. These results suggest that the Ets-1 PNT domain functions in heterotypic protein interactions and support the possibility that target recognition is coupled to structuring of the MAP kinase site.

About this Structure

2JV3 is a Single protein structure of sequence from Mus musculus. This structure supersedes the now removed PDB entry 1BQV. Full crystallographic information is available from OCA.

Reference

Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site., Slupsky CM, Gentile LN, Donaldson LW, Mackereth CD, Seidel JJ, Graves BJ, McIntosh LP, Proc Natl Acad Sci U S A. 1998 Oct 13;95(21):12129-34. PMID:9770451

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