| First Author | Johnson Philip E | Year | 2006 |
| Journal | Nat Struct Mol Biol | Volume | 13 |
| Pages | 177-8 | PubMed ID | 16429155 |
| Abstract Text | The putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p-SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop. | Doi | 10.1038/nsmb1039 |
| Issue | 2 | Month | Feb |
