Xiaoping Zhang, Pornpimon Angkasekwinai, Chen Dong, Hong Tang. Structure and function of interleukin-17 family cytokines[J]. Protein&Cell, 2011, 2(1): 26-40. doi: 10.1007/s13238-011-1006-5
Citation:
|
Xiaoping Zhang, Pornpimon Angkasekwinai, Chen Dong, Hong Tang. Structure and function of interleukin-17 family cytokines[J]. Protein&Cell, 2011, 2(1): 26-40. doi: 10.1007/s13238-011-1006-5
|
Xiaoping Zhang, Pornpimon Angkasekwinai, Chen Dong, Hong Tang. Structure and function of interleukin-17 family cytokines[J]. Protein&Cell, 2011, 2(1): 26-40. doi: 10.1007/s13238-011-1006-5
Citation:
|
Xiaoping Zhang, Pornpimon Angkasekwinai, Chen Dong, Hong Tang. Structure and function of interleukin-17 family cytokines[J]. Protein&Cell, 2011, 2(1): 26-40. doi: 10.1007/s13238-011-1006-5
|
Structure and function of interleukin-17 family cytokines
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1 Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;
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2 Department of Medical Technology, Faculty of Allied Health Sciences, Thammasat University, Pathum-thani 12121, Thailand;
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3 Department of Immunology, University of Texas and MD Anderson Cancer Center, Houston, Texas 77030, USA;
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4 The Graduate School of Chinese Academy of Sciences, Beijing 100101, China
- Received Date: 2010-12-28
- Rev Recd Date:
2010-12-28
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Abstract
The recently identified interleukin-17 (IL-17) cytokines family, which comprises six members in mammals (IL-17A-F), plays essential roles in the host immunity against infectious diseases and chronic inflammatory diseases. The three-dimensional structures containing IL-17A or IL-17F have become available and revealed the unique structural features of IL-17s as well as their receptors. Molecular modeling in this review shows that IL-17s may adopt a "cysteine knot" fold commonly seen in nerve growth factor (NGF) and other neurotrophins. Further modeling analysis unmasks a signature interaction feature of the IL-17F/IL-17RA complex, where a small loop of IL-17RA slots into the deep groove of the interface of IL-17F homodimer. This is quite different from the interaction between the best known four-helix cytokines and their cognate receptors. On the other hand, structure of IL-17A and its monoclonal antibody (CAT-2200) shows that, albeit that the antigenic epitope of IL-17A resides outside of the IL-17A homodimer interface, its physical proximity to the receptor binding groove may explain that antibody blockage would be achieved by interfering with the ligand-receptor interaction. This review is to summarize the advance in understanding the structure and function of IL-17 family cytokines, focusing mainly on IL-17A, IL-17F and IL-17E, in the hope of gaining better knowledge of immunotherapeutic strategies against various inflammatory diseases.
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References
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Proportional views
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