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• W2025611643 abstract "We compared three crystal structures of human interleukin 5 (hIL5) expressed in either E. coli (hIL5 E.coli ), Sf9 cells (hIL5 Sf9 ) or Drosophila cells (hIL5 Drosophila ). The dimeric hIL5 structures show subtle but significant conformational differences which are probably a consequence of the different crystallization conditions trapping this protein into one of two states. We refer to these two distinct conformations as the `open' and `tight' state, according to the packing around the cleft between the two subunits. We hypothesize that these two stable conformational states reflect the structure of the free or receptor bound hIL5." @default.
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• W2025611643 date "1998-03-13" @default.
• W2025611643 modified "2023-10-14" @default.
• W2025611643 title "Analysis of three human interleukin 5 structures suggests a possible receptor binding mechanism" @default.
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• W2025611643 doi "https://doi.org/10.1016/s0014-5793(98)00146-x" @default.
• W2025611643 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9539134" @default.
• W2025611643 hasPublicationYear "1998" @default.
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