Sequence and structural analysis of 4SNc-Tudor domain protein from Takifugu Rubripes |
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Authors: | Jianzhou Zheng Jian Lu Haijun Liu Jun Li Keping Chen |
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Institution: | 1.Institute of life science, Jiangsu University, Zhenjiang, China;2.Physical and Chemical Analysis Center, Jiangsu University, Zhenjiang, China |
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Abstract: | The fugu SN4TDR protein belongs to an evolutionarily conserved family, consisting of four repeat staphylococcal nuclease-like domains
(SN1-SN4) at the N-terminus followed by Tudor and SN-like domains (TSN). Sequence analysis showed that the C-terminal TSN domain is
composed of a complete SN-like domain interdigitated with a Tudor domain. In despite of low level of sequence identities, five SN-like
domains have a few conserved amino acids that may play essential roles in the function of the protein. Computer modeling and secondary
structural prediction of the SN-like domains revealed the presence of similar structural features of β1-β2-β3-α1-β4-β5-α2-α3, which provides
a structural basis for oligonucleotides binding. The loop region L3α for binding sites between β3 and α1 of SN-like domains are different
from human p100, implying the divergence in the structures of binding sites. These results indicate that fugu SN4TDR may bind methylated
ligands and/or oligonucleotides through its distant domains. |
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Keywords: | Takifugu rubripes SN4TDR SN-like domain Tudor domain |
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