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TitleBipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal.
Journal, issue, pagesNucleic Acids Res., Vol. 50, Page 536-548, Year 2022
Publish dateAug 28, 2021 (structure data deposition date)
AuthorsQiu, C. / Wine, R.N. / Campbell, Z.T. / Hall, T.M.T.
External linksNucleic Acids Res. / PubMed:34908132
MethodsX-ray diffraction
Resolution2.34 - 2.39 Å
Structure data

PDB-7rzz:
Crystal structure of FBF-2 in complex with LST-1 site A peptide and compact FBE RNA
Method: X-RAY DIFFRACTION / Resolution: 2.39 Å

PDB-7s02:
Crystal structure of FBF-2 in complex with LST-1 site A peptide and FBE RNA
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • caenorhabditis elegans (invertebrata)
KeywordsRNA BINDING PROTEIN / Pumilio RNA-binding proteins

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