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Structure paper

TitleArtificial ligand binding within the HIF2alpha PAS-B domain of the HIF2 transcription factor.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 106, Page 450-455, Year 2009
Publish dateOct 28, 2008 (structure data deposition date)
AuthorsScheuermann, T.H. / Tomchick, D.R. / Machius, M. / Guo, Y. / Bruick, R.K. / Gardner, K.H.
External linksProc. Natl. Acad. Sci. USA / PubMed:19129502
MethodsX-ray diffraction
Resolution1.17 - 1.598 Å
Structure data

PDB-3f1n:
Crystal structure of a high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains, with internally bound ethylene glycol.
Method: X-RAY DIFFRACTION / Resolution: 1.479 Å

PDB-3f1o:
Crystal structure of the high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains, with an internally-bound artificial ligand
Method: X-RAY DIFFRACTION / Resolution: 1.598 Å

PDB-3f1p:
Crystal structure of a high affinity heterodimer of HIF2 alpha and ARNT C-terminal PAS domains
Method: X-RAY DIFFRACTION / Resolution: 1.17 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-2XY:
N-[2-nitro-4-(trifluoromethyl)phenyl]morpholin-4-amine

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / PAS domain / heterodimer / internal cavity / Activator / Angiogenesis / Congenital erythrocytosis / Developmental protein / Differentiation / Disease mutation / DNA-binding / Hydroxylation / Nucleus / Phosphoprotein / Transcription regulation / Ubl conjugation / Alternative splicing / Polymorphism

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