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Molecules 2017, 22(7), 1229;

Effects of K11R and G31P Mutations on the Structure and Biological Activities of CXCL8: Solution Structure of Human CXCL8(3-72)K11R/G31P

Institute of Biotechnology and Department of Medical Science, National Tsing Hua University, Hsinchu 300, Taiwan
Division of Respirology, Critical Care and Sleep Medicine, Department of Medicine, University of Saskatchewan, Saskatoon, SK S7N 5B4, Canada
Department of Immunology, Dalian Medical University, Dalian 116044, China
Authors to whom correspondence should be addressed.
Received: 21 June 2017 / Revised: 18 July 2017 / Accepted: 19 July 2017 / Published: 21 July 2017
(This article belongs to the Special Issue Recent Advances in Biomolecular NMR Spectroscopy)
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The ELR-CXC chemokines are important to neutrophil inflammation in many acute and chronic diseases. Among them, CXCL8 (interleukin-8, IL-8), the expression levels of which are elevated in many inflammatory diseases, binds to both the CXCR1 and CXCR2 receptors with high affinity. Recently, an analogue of human CXCL8, CXCL8(3–72)K11R/G31P (hG31P) has been developed. It has been demonstrated that hG31P is a high affinity antagonist for both the CXCR1 and CXCR2. Herein, we have determined the solution structure and the CXCR1 N-terminal peptide binding sites of hG31P by NMR spectroscopy. We have found that the displacement within the tertiary structure of the 30 s loop and the N-terminal region and more specifically change of the loop conformation (especially H33), of hG31P may affect its binding to the CXCR1 receptor and thereby inhibit human neutrophil chemotactic responses induced by ELR-CXC chemokines. Our results provide a structural basis for future clinical investigations of this CXCR1/CXCR2 receptor antagonist and for the further development of CXCL8 based antagonists. View Full-Text
Keywords: CXCL8; antagonist; NMR; structure; mutation CXCL8; antagonist; NMR; structure; mutation

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Cheng, H.-T.; Yu, H.-Y.; Gordon, J.R.; Li, F.; Cheng, J.-W. Effects of K11R and G31P Mutations on the Structure and Biological Activities of CXCL8: Solution Structure of Human CXCL8(3-72)K11R/G31P. Molecules 2017, 22, 1229.

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