3NJ5

Crystal structure of chicken IL-1 hydrophobic cavity mutant 157

3NJ5 の概要

• エントリーDOI: 10.2210/pdb3nj5/pdb
• 分子名称: IL-1 beta (2 entities in total)
• 機能のキーワード: chicken, interleukin-1 beta, hydrophobic cavity mutant, cytokine
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18059.58

構造登録者

Yin, H.S.,Chen, Y.W. (登録日: 2010-06-17, 公開日: 2011-06-22, 最終更新日: 2024-03-20)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.67 Å)