2jv3
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The Pointed (PNT) domain and an adjacent mitogen-activated protein (MAP) | + | 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== | ==About this Structure== | ||
| - | 2JV3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure | + | 2JV3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry 1BQV. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kang, H.]] | [[Category: Kang, H.]] | ||
| - | [[Category: Lawrence, M | + | [[Category: Lawrence, M P.]] |
| - | [[Category: Lee, G | + | [[Category: Lee, G M.]] |
[[Category: Schaerpf, M.]] | [[Category: Schaerpf, M.]] | ||
| - | [[Category: Slupsky, C | + | [[Category: Slupsky, C M.]] |
[[Category: alpha-helical bundle]] | [[Category: alpha-helical bundle]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:06:08 2008'' |
Revision as of 16:06, 21 February 2008
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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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