9SBF

Drosophila Elav, eSH3 fragment (RRM3) - hexagonal crystal form

Summary for 9SBF

• Entry DOI: 10.2210/pdb9sbf/pdb
• Descriptor: Protein elav (1 entity in total)
• Functional Keywords: rna recognition, rna binding protein
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 4
• Total formula weight: 46072.78

Authors

Futterer, K.,Soller, M. (deposition date: 2025-08-08, release date: 2026-06-17, Last modification date: 2026-10-14)

Primary citation

Dix, T.C.,McQuarrie, D.W.J.,Brauer, U.,Tian, Y.W.,Haussmann, I.U.,Li, M.,Futterer, K.,Soller, M.
Multimerization of ELAV in Drosophila is essential for directing neuronal alternative splicing and polyadenylation programs.
Genes Dev., 40:1669-1687, 2026

PubMed Abstract: ELAV/Hu RNA-binding proteins (RBPs) are key regulators of neuronal alternative splicing and polyadenylation programs across animals. How ELAV/Hu RBPs achieve gene-specific regulation by recognizing spaced U-rich motifs through multimerization, remains uncertain. We determined X-ray crystal structures of ELAV RNA recognition motif 3 (RRM3) to reveal that multimerization is mediated by two evolutionarily conserved interfaces in non-RNA-binding parts of the RRM to form a tetramer and RNA binding is not required for multimerization. Mutational probing of these two interfaces in photoreceptor neurons shows that both interfaces contribute to ELAV function in development. Notably, multimerization defective mutants are embryonic lethal. Genomic profiling demonstrates that multimerization is required to direct neuronal alternative splicing and polyadenylation programs of some, but not all ELAV target genes. Our study provides a structural basis for a mechanistic understanding how ELAV/Hu proteins can extract gene-specific regulation from a landscape of redundant sequence motifs.

PubMed: 42580850
DOI: 10.1101/gad.353688.126

Experimental method

X-RAY DIFFRACTION (3.73 Å)