1sxe: Difference between revisions

Revision as of 15:08, 29 July 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:1sxe.png

Template:STRUCTURE 1sxe

The solution structure of the Pointed (PNT) domain from the transcrition factor ErgThe solution structure of the Pointed (PNT) domain from the transcrition factor Erg

Template:ABSTRACT PUBMED 15351649

About this StructureAbout this Structure

1SXE is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Diversity in structure and function of the Ets family PNT domains., Mackereth CD, Scharpf M, Gentile LN, MacIntosh SE, Slupsky CM, McIntosh LP, J Mol Biol. 2004 Sep 24;342(4):1249-64. PMID:15351649

Page seeded by OCA on Tue Jul 29 15:07:56 2008

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

OCA

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-'''The solution structure of the Pointed (PNT) domain from the transcrition factor Erg'''
+===The solution structure of the Pointed (PNT) domain from the transcrition factor Erg===
-==Overview==
+<!--
-The PNT (or Pointed) domain, present within a subset of the Ets family of transcription factors, is structurally related to the larger group of SAM domains through a common tertiary arrangement of four alpha-helices. Previous studies have shown that, in contrast to the PNT domain from Tel, this domain from Ets-1 contains an additional N-terminal helix integral to its folded structure. To further investigate the structural plasticity of the PNT domain, we have used NMR spectroscopy to characterize this domain from two additional Ets proteins, Erg and GABPalpha. These studies both define the conserved and variable features of the PNT domain, and demonstrate that the additional N-terminal helix is also present in GABPalpha, but not Erg. In contrast to Tel and Yan, which self-associate to form insoluble polymers, we also show that the isolated PNT domains from Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Pnt-P2 are monomeric in solution. Furthermore, these soluble PNT domains do not associate in any pair-wise combination. Thus these latter Ets family PNT domains likely mediate interactions with additional components of the cellular signaling or transcriptional machinery.
+The line below this paragraph, {{ABSTRACT_PUBMED_15351649}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15351649 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15351649}}
 ==About this Structure==
-SXE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SXE OCA].
+SXE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SXE OCA].
 ==Reference==
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 [[Category: Slupsky, C M.]]
 [[Category: Alpha helical]]
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