Matches in SemOpenAlex for { <https://semopenalex.org/work/W4321350377> ?p ?o ?g. }
- W4321350377 abstract "ABSTRACT Drosophila Smaug and its orthologs comprise a family of mRNA repressor proteins that exhibit various functions during animal development. Smaug proteins contain a characteristic RNA-binding sterile-α motif (SAM) domain and a conserved but uncharacterized N-terminal domain (NTD). Here, we resolved the crystal structure of the NTD of the human SAM domain-containing protein 4A (SAMD4A, a.k.a. Smaug1) to 2.0 Å resolution, which revealed its composition of a homodimerization D-subdomain and a subdomain with similarity to a PHAT domain. Furthermore, we show that Drosophila Smaug directly interacts with the Drosophila germline inducer Oskar and with the Hedgehog signaling transducer Smoothened through its D-PHAT domain. We determined the crystal structure of the D-PHAT domain of Smaug in complex with a Smoothened α-helical peptide to 1.61 Å resolution. The peptide binds within a groove that is formed by both the D- and PHAT subdomains. Structural modeling supported by experimental data suggested that an α-helix within the disordered region of Oskar binds to the D-PHAT domain in a mode similar to Smoothened. Together, our data uncover the N-terminal D-PHAT domain of Smaug as peptide-binding domain." @default.
- W4321350377 created "2023-02-20" @default.
- W4321350377 creator A5000984993 @default.
- W4321350377 creator A5026568220 @default.
- W4321350377 creator A5062439581 @default.
- W4321350377 creator A5069153156 @default.
- W4321350377 date "2023-02-19" @default.
- W4321350377 modified "2023-09-30" @default.
- W4321350377 title "Structural basis for binding of Smaug to the GPCR Smoothened and to the germline inducer Oskar" @default.
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- W4321350377 doi "https://doi.org/10.1101/2023.02.19.529116" @default.
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