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Structure paper

TitleThe mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 16, Page 247-254, Year 2009
Publish dateDec 9, 2008 (structure data deposition date)
Authorsvon Moeller, H. / Basquin, C. / Conti, E.
External linksNat. Struct. Mol. Biol. / PubMed:19219046
MethodsX-ray diffraction
Resolution2.2 - 2.8 Å
Structure data

PDB-3fhc:
Crystal structure of human Dbp5 in complex with Nup214
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3fht:
Crystal structure of human Dbp5 in complex with AMPPNP and RNA
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN/HYDROLASE / DEAD-box helicase / mRNA export / Nucleoporin / beta propeller / RecA-like / RNA dependent ATPase / CAN / Ddx19 / Dead-box protein 19b / nuclear pore complex / Glycoprotein / mRNA transport / Nucleus / Phosphoprotein / Protein transport / Proto-oncogene / Translocation / Transport / ATP-binding / Helicase / Hydrolase / Membrane / Nucleotide-binding / RNA-binding / TRANSPORT PROTEIN-HYDROLASE COMPLEX / HYDROLASE/RNA / Dbp5 / nucleocytoplasmic transport / Nup214 / Nup159 / DDX19b / nuclear pore / gle1 / HYDROLASE-RNA COMPLEX

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