Abstract
The TGF-β superfamily consists of an expanding number of structurally similar proteins which have been implicated in the regulation of a variety of cellular processes such as growth, motility, and differentiation. Members of the TGF-β superfamily have been classified into major family groupings on the basis of homologies within a seven cysteine domain which encompasses most of the mature protein [1–4]. These include TGF-β, bone morphogenetic protein (BMP), growth and differentiation factor (GDF), inhibin-b/activin (inhB), inhibin-α (inhA), mullerian inhibitory substance (MIS), and glial derived neurotrophic factor (GDNF). The highly characteristic secondary and tertiary structure of TGF-β superfamily proteins occurs within the seven cysteine domain [1–4], even though the level of sequence homology between disparate family members can be low [5], The knotted structure generated by the highly conserved pattern and spacing of cysteine residues leads to dimeric proteins of remarkable stability. This highly conserved structure also makes it relatively simple to identify new members of this superfamily.
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Moore, A.G. et al. (2001). MIC-1 and other TGF-β superfamily members in inflammation. In: Breit, S.N., Wahl, S.M. (eds) TGF-β and Related Cytokines in Inflammation. Progress in Inflammation Research. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8354-2_1
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DOI: https://doi.org/10.1007/978-3-0348-8354-2_1
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