2WRY

Crystal structure of chicken cytokine interleukin 1 beta

Summary for 2WRY

• Entry DOI: 10.2210/pdb2wry/pdb
• Descriptor: INTERLEUKIN-1BETA (2 entities in total)
• Functional Keywords: immune system, pyrogen, mitogen, inflammatory response
• Biological source: GALLUS GALLUS (CHICKEN)
• Total number of polymer chains: 1
• Total formula weight: 18075.58

Authors

Lu, W.S.,Cheng, C.S.,Lyu, P.C.,Lee, L.H.,Wang, W.C.,Yin, H.S. (deposition date: 2009-09-03, release date: 2010-09-29, Last modification date: 2023-12-20)

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-, 2011

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: 21288573
DOI: 10.1016/J.MOLIMM.2011.01.002

Experimental method

X-RAY DIFFRACTION (1.58 Å)