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Analysis of three human interleukin 5 structures suggests a possible receptor binding mechanism
Author(s) -
Verschelde J.-L,
Ampe C,
Guisez Y,
Oefner C,
Vandekerckhove J,
Tavernier J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00146-x
Subject(s) - sf9 , chemistry , mechanism (biology) , conformational change , receptor , biophysics , crystallization , protein structure , crystallography , stereochemistry , biology , biochemistry , physics , recombinant dna , gene , organic chemistry , quantum mechanics , spodoptera
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.