3NJ5
Crystal structure of chicken IL-1 hydrophobic cavity mutant 157
Summary for 3NJ5
| Entry DOI | 10.2210/pdb3nj5/pdb |
| Descriptor | IL-1 beta (2 entities in total) |
| Functional Keywords | chicken, interleukin-1 beta, hydrophobic cavity mutant, cytokine |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 18059.58 |
| Authors | Yin, H.S.,Chen, Y.W. (deposition date: 2010-06-17, release date: 2011-06-22, Last modification date: 2024-03-20) |
| Primary citation | Cheng, C.S.,Chen, W.T.,Lee, L.H.,Chen, Y.W.,Chang, S.Y.,Lyu, P.C.,Yin, H.S. Structural and functional comparison of cytokine interleukin-1 beta from chicken and human Mol.Immunol., 48:947-955, 2011 Cited by PubMed Abstract: Interleukin-1 beta (IL-1β) is an important cytokine in the immune system. The properties of avian IL-1βs are less well understood than the mammalian IL-1βs, and there is no available structure of avian IL-1βs in the Protein Data Bank. Here, we report the crystal structures of wild-type and Y157F mutant IL-1βs from chicken. Both the wild-type and mutant IL-1βs share a beta-trefoil conformation similar to that of human IL-1β and also have an internal hydrophobic cavity. However, the cavity sizes clearly differ from that of human IL-1β due to the packing of hydrophobic residues. Our studies also reveal that the relative thermal stability of IL-1βs does not correlate with cavity size but rather is dependent on the amino acid residues present around the cavity. This cavity serves as a scaffold for maintaining the structure of the IL-1β core region but does not have a biological function per se. Moreover, we found that human IL-1β cannot induce chemokine expression in chicken fibroblasts or elevate plasma cortisol levels in chickens, implying a lack of cross-species bioactivity. Close examination reveals that significant structural and sequence differences occur in the terminal and some loop regions between human and chicken IL-1βs. These variable regions have been shown to be critical for receptor binding, thus resulting in a lack of species cross-reactivity between human and chicken IL-1β. PubMed: 21288573DOI: 10.1016/j.molimm.2011.01.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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