Comparative analysis of receptor binding by chicken and human interleukin-1β.
Interleukin-1β (IL-1β) is an important cytokine in the immune system. Mammalian and avian IL-1βs share only 31-35% sequence identity, and the function of avian IL-1βs is less well understood by comparison. Although chicken and mammalian IL-1βs have similar tertiary structures, these ILs differ significantly with respect to receptor activation. Analysis of the structures and sequences of IL-1βs reveals that the major differences lie in loops. Modeling docking of chicken IL-1β to its receptor reveals that these variable loops are critical for receptor binding. Molecular dynamics simulations of the IL-1βs reveal significant changes in the dynamic range of motion upon receptor binding. Loops 3 and 9 of the unbound chicken IL-1β had greater fluctuations compared with the other loops. Upon binding, the flexibility of these loops, which directly contact the receptor, markedly decreases. Taken together, these results suggest that receptor binding leads to not only favorable enthalpy but also lower conformational entropy.
Cheng
Chao-Sheng
CS
Institute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Lu
Wen-Shiang
WS
Tu
I-Fan
IF
Lyu
Ping-Chiang
PC
Yin
Hsien-Sheng
HS
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D017124:Conserved Sequence; D006801:Humans; D006860:Hydrogen Bonding; D053590:Interleukin 1 Receptor Antagonist Protein / Q000737:chemistry; D053582:Interleukin-1alpha / Q000737:chemistry; D053583:Interleukin-1beta / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017472:Receptors, Interleukin-1 / Q000737:chemistry*; D016415:Sequence Alignment
D053590:Interleukin 1 Receptor Antagonist Protein; D053582:Interleukin-1alpha; D053583:Interleukin-1beta; D017472:Receptors, Interleukin-1
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