1sxe: Difference between revisions
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'''The solution structure of the Pointed (PNT) domain from the transcrition factor Erg''' | {{Structure | ||
|PDB= 1sxe |SIZE=350|CAPTION= <scene name='initialview01'>1sxe</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= ERG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''The solution structure of the Pointed (PNT) domain from the transcrition factor Erg''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1SXE is a [ | 1SXE 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]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15351649 15351649] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha helical]] | [[Category: alpha helical]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:10:59 2008'' | ||
Revision as of 15:11, 20 March 2008
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| Gene: | ERG (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The solution structure of the Pointed (PNT) domain from the transcrition factor Erg
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Lathosterolosis OMIM:[602286]
About this StructureAbout this Structure
1SXE is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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
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