Abstract.
Extracellular domains of some cellular receptors expressed in the organisms at different levels of development belong to three-fingered protein (TFP) fold. The Homo sapiens genome encodes at least 45 genes containing from one to three TFP domains (TFPDs), namely diverse paralogues of the Ly6 gene, CD59 and the receptors of activins, bone morphogenetic proteins, Mullerian inhibiting substance and transforming growth factor-β. C4.4a and urokinase/plasminogen activatory receptor contain two and three TFPD repeats, respectively. These diverse proteins have a low overall sequence similarity with each other and their hydrophobicity levels vary to a considerable degree. It is suggested that sequence differentiation within the TFPD led to distinct groups of proteins whose attributes were optimized to fit both the physicochemical properties specific to their functional microenvironment and selective targeting of their highly diversified extracellular cofactors.
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Received 7 August 2008; accepted 29 August 2008
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Figure 1S. Dendrogram derived from the alignment of all the human TFPDs shown in Table 1. Attention: some of the branches were probably correctly set up, e.g., the ECDs of the TGFβ family of receptors that perhaps are due to gene duplication events. Arrangements of the other branches are less certain since the IDs were relatively low in this group of protein domains.
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Figure 2S. (A) Distribution of the IDs in the MSA802; (B) Ie values calculated from the MSA802. The Cys residues were explicitly placed on the graph with the highly conserved positions indicated by the arrows. The following disulfide bonds are formed: C1-C3 (Db1), C2-C4 (Db2), C5-C6 (Db3), C7-C8 (Db4), and C1a-C1b (Db1a disulfide bond in Finger 1).
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Galat, A. The three-fingered protein domain of the human genome. Cell. Mol. Life Sci. 65, 3481–3493 (2008). https://doi.org/10.1007/s00018-008-8473-8
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DOI: https://doi.org/10.1007/s00018-008-8473-8