7nyq | pdb_00007nyq

Crystal structure of the Mei-P26 NHL domain

spinqualitylabelsall models 7nyq, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7nyq is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The TRIM-NHL protein Meiotic P26 (Mei-P26) acts as a regulator of cell fate in Drosophila Its activity is critical for ovarian germline stem cell maintenance, differentiation of oocytes, and spermatogenesis. Mei-P26 functions as a post-transcriptional regulator of gene expression; however, the molecular details of how its NHL domain selectively recognizes and regulates its mRNA targets have remained elusive. Here, we present the crystal structure of the Mei-P26 NHL domain at 1.6 A resolution and identify key amino acids that confer substrate specificity and distinguish Mei-P26 from closely related TRIM-NHL proteins. Furthermore, we identify mRNA targets of Mei-P26 in cultured Drosophila cells and show that Mei-P26 can act as either a repressor or activator of gene expression on different RNA targets. Our work reveals the molecular basis of RNA recognition by Mei-P26 and the fundamental functional differences between otherwise very similar TRIM-NHL proteins. Molecular insights into RNA recognition and gene regulation by the TRIM-NHL protein Mei-P26.,Salerno-Kochan A, Horn A, Ghosh P, Nithin C, Koscielniak A, Meindl A, Strauss D, Krutyholowa R, Rossbach O, Bujnicki JM, Gaik M, Medenbach J, Glatt S Life Sci Alliance. 2022 May 5;5(8). pii: 5/8/e202201418. doi:, 10.26508/lsa.202201418. Print 2022 Aug. PMID:35512835 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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