1A9N

CRYSTAL STRUCTURE OF THE SPLICEOSOMAL U2B''-U2A' PROTEIN COMPLEX BOUND TO A FRAGMENT OF U2 SMALL NUCLEAR RNA

Summary for 1A9N

• Entry DOI: 10.2210/pdb1a9n/pdb
• Descriptor: RNA (5'-R(*CP*CP*UP*GP*GP*UP*AP*UP*UP*GP*CP*AP*GP*UP*AP*CP*CP*UP*CP*CP*AP*GP* GP*U)-3'), U2A', SPLICEOSOMAL U2B'' (3 entities in total)
• Functional Keywords: complex (nuclear protein-rna), rna, snrnp, ribonucleoprotein, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P09661 P08579
• Total number of polymer chains: 6
• Total formula weight: 77996.36

Authors

Price, S.R.,Evans, P.R.,Nagai, K. (deposition date: 1998-04-08, release date: 1998-09-23, Last modification date: 2024-10-30)

Primary citation

Price, S.R.,Evans, P.R.,Nagai, K.
Crystal structure of the spliceosomal U2B"-U2A' protein complex bound to a fragment of U2 small nuclear RNA.
Nature, 394:645-650, 1998

PubMed Abstract: We have determined the crystal structure at 2.4 A resolution of a ternary complex between the spliceosomal U2B"/U2A' protein complex and hairpin-loop IV of U2 small nuclear RNA. Unlike its close homologue the U1A protein, U2B" binds to its cognate RNA only in the presence of U2A', which contains leucine-rich repeats in its sequence. The concave surface of a parallel beta-sheet within the leucine-rich-repeat region of U2A' interacts with the ribonucleoprotein domain of U2B" on the surface opposite its RNA-binding surface. The basic carboxy-terminal region of U2A' interacts with the RNA stem. The crystal structure reveals how protein-protein interaction regulates RNA-binding specificity, and how replacing only a few key residues allows the U2B" and U1A proteins to discriminate between their cognate RNA hairpins by forming alternative networks of interactions.

PubMed: 9716128
DOI: 10.1038/29234

Experimental method

X-RAY DIFFRACTION (2.38 Å)