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ISSN: 2157-7412

Journal of Genetic Syndromes & Gene Therapy
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Research Article

Identification of the Key Functional Domain of BAFF for Binding TACI by Computer-Guided Molecular Modeling Method

Ru Wang1,2, Zhou Lin1, Hui Peng1, Huawei Wei1, Xinying Li1, Jian Sun3, Jianmin Fang4, Ning Li1, Xiangbin Meng1, Beifen Shen1, Jiannan Feng1* and Yan Li1*

1Laboratory of Immunology, Institute of Basic Medical Sciences, Beijing 100850, China

2Clinical laboratory,The 305 Hospital of People’s Liberation Army, Beijing 100017, China

3School of Pharmaceutical Science and Technology, TianJin University, Tianjin, 300072, China

4School of Life Sciences and Technology, Tong Ji University, Shanghai 200092, China

*Corresponding Author:
Jiannan Feng
Laboratory of Immunology Institute of Basic Medical Sciences
P.O. Box 130 (3)Taiping Road #27 Beijing 100850, China
Tel: +86-10-66931325
Fax: 86-10-68159436
E-mail: [email protected]
Yan Li
Laboratory of Immunology Institute of Basic Medical Sciences
P.O. Box 130 (3)Taiping Road #27 Beijing 100850, China
Tel: +86-10-66931325
Fax: 86-10-68159436
E-mail: [email protected]

Received date: April 28, 2012; Accepted date:May 24, 2012; Published date: May 28, 2012

Citation: Wang R, Lin Z, Peng H, Wei H, Li X, et al. (2012) Identification of the Key Functional Domain of BAFF for Binding TACI by Computer-Guided Molecular Modeling Method. J Genet Syndr Gene Ther 3:114. doi:10.4172/2157-7412.1000114

Copyright: © 2012 Wang R, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

 

Abstract

As an important member of the Tumor Necrosis Factor (TNF) super family, B cell activating factor (BAFF: also known as BLyS, TALL-1, THANK and zTNF4 or TNFSF13b) induces B cell proliferation and differentiation both in vivo and in vitro. A series of experimental results showed that the soluble form of a BAFF receptor, trans-membrane activator and CAML-interactor (TACI), could alleviate the autoimmune symptoms of NZBWF1 and MRL-lpr/lpr mice. Furthermore, the fusion protein TACI-Fc, as a novel BAFF antagonist, was used to the treatment of relapsing multiple sclerosis. However, it is not clear how BAFF interact with its receptor TACI. In this study, using the crystal structures of BAFF and its receptor TACI, the binding mode and the key domains of BAFF interaction with TACI were analyzed based on the computer-guided molecular modeling method. According to the theoretical predictions, a series of mutants of BAFF, including M1 (from Ile158 to Phe165), M2 (from Asp203 to Leu211), M3 (from Ser225 to Arg231) and M4 (from Ile233 to Glu238), were designed and evaluated with biological experiments. The results showed that the domains M2 and M4 of BAFF were the key domains interacting with TACI, which was in accord with our theoretical results. The results will highlight the clues for further development of novel BAFF inhibitors.

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