Blaine H. Gordon

This paper presents the NMR structure of HsLARP6's La domain bound to a 5' stem-loop RNA, revealing a non-canonical binding interface that enables specific recognition of structured RNA.

This paper describes a protocol to produce and purify the La domain of human LARP6, showing that RNA binding increases its stability and reduces aggregation.

This study identifies the RNK motif in LARP6's La-domain as critical for sequence-specific binding to the 5SL of collagen mRNAs, suggesting it as a target for antifibrotic drug design.