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From Proteopedia
Crystal Structure of human Translin
Structural highlights
Function[TSN_HUMAN] DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.[1] [2] Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand.[3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Structure of human translin at 2.2 A resolution.,Sugiura I, Sasaki C, Hasegawa T, Kohno T, Sugio S, Moriyama H, Kasai M, Matsuzaki T Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):674-9. Epub 2004, Mar 23. PMID:15039555[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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