| Summary: | 碩士 === 國立清華大學 === 生物科技研究所 === 95 === Abstract
Interleukin-8 (IL8), a kind of CXC chemokines with an ELR motif, was identified in 1987 as a novel type of neutrophil-activating cytokine. IL8 plays an important role in immune system because IL8 can induce inflammation response. IL8 is a molecular weight of 8.5 kDa protein with 72 amino acids. Professor John Gordon had proved that IL8(3-74) K11R/G31P mutation is a potential antagonist. Thus, we used human K11R/G31P as the subject to perform the structural studies. The backbone sequential assignments were accomplished from five triple resonance experiments (HNCA, HNCO, HN(CO)CA, CBCANH, and CBCA(CO)NH). Side chain assignments were obtained from TOCSY-HSQC, HCC(CO)NH and HCCH-TOCSY. Moreover, hydrogen-deuterium exchange experiments were achieved. Secondary structures were identified via NOE correlations, amide proton exchange and CSI analyses. Our results show that the secondary structure is similar to wild type IL8. The G31P mutation induced a local conformational change and the three-dimensional structure roughly displayed the divergent S30-A35 turn of K11R/G31P compared with wild type IL8. Thus, we suggested that this local conformational change is a possible influence making K11R/G31P antagonistic to wild type IL8.
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