Noncanonical RNA binding of human La-related protein 6.

ABSTRACT: La-related proteins (LARPs) are RNA-binding proteins that are involved in a variety of disease-related processes. Most LARPs recognize short single-stranded poly(U/A) motifs via a conserved hydrophobic pocket. Human LARP6 (HsLARP6) is an exception, binding a structured 5' stem-loop (5'SL) that controls type I collagen translation and fibroproliferative disease progression. Here, we present the de novo solution nuclear magnetic resonance structure of the La domain of HsLARP6 in the bound state. Chemical shift perturbation, solvent paramagnetic relaxation enhancement, intermolecular nuclear Overhauser effects, and targeted mutagenesis converge on a previously unknown binding interface that integrates electrostatic and hydrophobic contacts with shape complementarity in 5'SL binding. This nonc

SUBMITTER: Gordon BH 

PROVIDER: S-EPMC12288881 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature