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The structure of human translin at 2.2 A resolution is reported in space group C222(1). Translin forms a tetramer in the asymmetric unit. Although the monomer structure is almost the same as the crystal structure of murine translin in space group P2(1)2(1)2, the relative positions of the tetramers differ between the human and murine translins. This suggests that the multimerization of translin is flexible; the flexibility may be related to the binding to DNA/RNA.
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Sugiura et al. (2004) studied this question.
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