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|1urn, resolution 1.92Å ()|
U1A MUTANT/RNA COMPLEX + GLYCEROL
The crystal structure of the RNA-binding domain of the small nuclear ribonucleoprotein U1A bound to a 21-nucleotide RNA hairpin has been determined at 1.92 A resolution. The ten-nucleotide RNA loop binds to the surface of the beta-sheet as an open structure, and the AUUGCAC sequence of the loop interacts extensively with the conserved RNP1 and RNP2 motifs and the C-terminal extension of the RNP domain. These interactions include stacking of RNA bases with aromatic side chains of proteins and many direct and water-mediated hydrogen bonds. The structure reveals the stereochemical basis for sequence-specific RNA recognition by the RNP domain.
Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin., Oubridge C, Ito N, Evans PR, Teo CH, Nagai K, Nature. 1994 Dec 1;372(6505):432-8. PMID:7984237
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Oubridge C, Ito N, Evans PR, Teo CH, Nagai K. Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature. 1994 Dec 1;372(6505):432-8. PMID:7984237 doi:http://dx.doi.org/10.1038/372432a0
- Alm E, Morozov AV, Kortemme T, Baker D. Simple physical models connect theory and experiment in protein folding kinetics. J Mol Biol. 2002 Sep 13;322(2):463-76. PMID:12217703
- Greene LH, Higman VA. Uncovering network systems within protein structures. J Mol Biol. 2003 Dec 5;334(4):781-91. PMID:14636602
- Hicks JM, Hsu VL. The extended left-handed helix: a simple nucleic acid-binding motif. Proteins. 2004 May 1;55(2):330-8. PMID:15048824 doi:10.1002/prot.10630