Analysis of three human interleukin 5 structures suggests a possible receptor binding mechanism

FEBS Letters

Ampe, C¹  Vandekerckhove, J¹  Tavernier, J¹  Oefner, C³  Verschelde, J.-L¹  Guisez, Y² 

[1] Flanders' Interuniversity Institute for Biotechnology, Department of Medical Protein Research, University Ghent, Faculty of Medicine, K.L. Ledeganckstraat 35, 9000 Gent, Belgium;Roche Research Gent, Jozef Plateaustraat 22, 9000 Gent, Belgium;Department of Pharmaceutical Research, New Technologies, F. Hoffmann-La Roche, Basel, Switzerland

关键词: Interleukin;    Conformational change;    Domain motion;    Interleukin 5 α-receptor subunit;   

DOI  :  10.1016/S0014-5793(98)00146-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown