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Resonance assignment of human LARP4A La module

Research output: Contribution to journalArticlepeer-review

Isabel Cruz-Gallardo, Luigi Martino, Roberta Trotta, Stefano De Tito, Geoff Kelly, R Andrew Atkinson, Antonio Randazzo, Maria R Conte

Original languageEnglish
Pages (from-to)169-172
Number of pages4
JournalBiomolecular NMR Assignments
Issue number1
Early online date10 Jan 2019
Accepted/In press1 Jan 2019
E-pub ahead of print10 Jan 2019
Published1 Apr 2019

King's Authors


Human LARP4A belongs to a superfamily of RNA binding proteins called La-related proteins (LARPs). Whilst being a positive regulator of protein synthesis and a promoter of mRNA stability, LARP4A also controls cell morphology and motility in human breast and prostate cancer cells. All LARPs share a characteristic RNA binding unit named the La–module, which despite a high level of primary structure conservation exhibits a great versatility in RNA target selection. Human LARP4A La–module is the most divergent compared with other LARPs and its RNA recognition properties have only recently started to be revealed. Given the key role of LARP4A protein in cancer cell biology, we have initiated a complete NMR characterisation of its La-module and here we report the assignment of 1H, 15N and 13C resonances resulting from our studies.

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