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. 2025 Jun;19(1):165-173.
doi: 10.1007/s12104-025-10232-7. Epub 2025 Apr 30.

1H, 13C, and 15N resonance assignment of the 5'SL-bound La domain of the human La-related protein 6

Blaine H Gordon  1   2 , Robert Silvers  3   4
Affiliations

1H, 13C, and 15N resonance assignment of the 5'SL-bound La domain of the human La-related protein 6

Blaine H Gordon et al. Biomol NMR Assign. 2025 Jun.

Abstract

Human La-related protein 6 (HsLARP6) participates in the post-transcriptional regulation of type I collagen biosynthesis and is involved in the onset and progression of fibroproliferative disease. The RNA-binding protein HsLARP6 recognizes a hairpin structure known as the 5' stem-loop (5'SL) located at the junction of 5' untranslated and coding regions of type I collagen mRNA. Despite extensive biochemical and functional studies of the interaction between HsLARP6 and the 5'SL motif, the lack of high-resolution molecular data significantly hampers our understanding of the binding mechanism. Here, we introduced a shorter 5'SL model, named A2M5, reducing the molecular size of the protein-RNA complex as well as spectral overlap in RNA-based spectra. Furthermore, we reported the near-complete backbone and side chain resonance assignment of the La domain of HsLARP6 in a 1:1 complex with the A2M5 model RNA. These results will provide a significant platform for future NMR spectroscopic studies of 5'SL binding to the La domain of HsLARP6.

Keywords: 5’SL; Fibrosis; LARP; La-related protein 6; Type I collagen.

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Conflict of interest statement

Declarations. Competing interests: The authors declare no competing interests.

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