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QuickView for DZF domain (biogroup)
- Description:
- This entry represents the DZF domain, which is foundexclusively in the metazoa.The DZF domain (domain associated with zinc fingers) is a dimerisation domainfound in:Vertebrate nuclear factor 90 (NF90, also known as ILF3, DRBP76 or NFAR-1), contains two double-stranded RNA-binding motifs (dsRBMs) and interacts with highly structured RNAs as well as the dsRNA-activated protein kinase (PKR). Metazoan NF45 (also known as ILF2), appears to function predominantly as a heterodimeric complex with NF90. Vertebrate spermatid perinuclear RNA-binding protein (SPNR, also known as STRBP), a testes specific paralogue of NF90. Metazoan Zinc-finger protein associated with RNA (Zfr).Nuclear factors NF90 and NF45 form a protein complex involved in a variety ofcellular processes and are thought to affect gene expression both at thetranscriptional and translational level. In addition, this complex affects thereplication of several viruses through direct interactions with viral RNA.NF90 and NF45 dimerize through their common DZF domain. The DZF domain showsstructural similarity to the template-free nucleotidyltransferase family ofRNA modifying enzymes. However, the lack of conserved catalytic residuessuggests that the DZF domain encodes a 'pseudotransferase' that is no longerable to catalyze transfer of nucleotides.The DZF dimerisation domain form an oblong structure with a flat face on oneside and a curved face on the other. The DZF domain is bipartite andcharacterised by an N-terminal mixed alpha-beta region that contains a centralanti-parallel beta-sheet and a C-terminal alpha-helical region. The overall structure has a pseudo two-fold rotational symmetry.The central beta-sheet forms the base of a cleft between the N- and C-terminalhalves while dimerization is mediated by the alpha-helices at the C terminus.
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