2jv3: Difference between revisions

Revision as of 12:16, 20 August 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2jv3.png

Template:STRUCTURE 2jv3

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

Template:ABSTRACT PUBMED 9770451

About this StructureAbout this Structure

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

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2jv3|  PDB=2jv3  |  SCENE=  }}
-'''Ets-1 PNT domain (29-138) NMR structure ensemble'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9770451}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9770451 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9770451}}
 ==About this Structure==
-JV3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bqv 1bqv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV3 OCA].
+JV3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bqv 1bqv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV3 OCA].
 ==Reference==
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 [[Category: Nucleus]]
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