6j9r | pdb_00006j9r

Coiled-coil Domain of Drosophila TRIM Protein Brat

spinqualitylabelsall models 6j9r, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6j9r is a 2 chain structure with sequence from Drosophila melanogaster american nodavirus (anv) sw-2009a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL NonStd Res: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BRAT_DROME] Plays a central role in translation repression of hb mRNA by being recruited by nos and pum to the Nanos Response Element (NRE), a 16 bp sequence in the hb mRNA 3'-UTR. Probably recruited by other proteins to repress translation of other mRNAs in other tissues. Involved in the regulation of ribosomal RNA synthesis and cell growth. Participates in abdominal segmentation and imaginal disk development. Involved in brain tumor suppression, by acting as a growth suppressor in the larval brain. Publication Abstract from PubMed Drosophila brain tumor (Brat) is a translational repressor belonging to the tripartite motif (TRIM) protein superfamily. During the asymmetric division of Drosophila neuroblasts, Brat localizes at the basal cortex via direct interaction with the scaffolding protein Miranda (Mira), and segregates into the basal ganglion mother cells after cell division. It was previously reported that both the coiled-coil (CC) and NHL domains of Brat are required for the interaction with Mira, but the underlying structural basis is elusive. Here, we determine the crystal structure of Brat-CC domain (aa 376-511) at 2.5 A, showing that Brat-CC forms an elongated antiparallel dimer through an unconventional CC structure. The dimeric assembly in Brat-CC structure is similar to its counterparts in other TRIM proteins, but Brat-CC also exhibits some distinct structural features. We also demonstrate that the CC domain could not bind Mira by its own, neither does the isolated NHL domain of Brat. Rather, Brat binds to Mira through the CC-NHL domain tandem, indicating that the function of the CC domain is to assemble Brat-NHL in dimeric form, which is necessary for Mira binding. Crystal structure of the coiled-coil domain of Drosophila TRIM protein Brat.,Liu C, Shan Z, Diao J, Wen W, Wang W Proteins. 2019 Apr 8. doi: 10.1002/prot.25691. PMID:30958583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA