Nature. 1990 Dec 6;348(6301):515-20.

Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A.

Nagai K, Oubridge C, Jessen TH, Li J, Evans PR.

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MRC Laboratory of Molecular Biology, Cambridge, UK.

Abstract

The crystal structure of the RNA binding domain of the U1 small nuclear ribonucleoprotein A, which forms part of the ribonucleoprotein complex involved in the excision of introns, has been solved. It contains a four-stranded beta sheet and two alpha helices. The highly conserved segments designated RNP1 and RNP2 lie side by side on the middle two beta strands. U1 RNA binding studies of mutant proteins suggest that the RNA binds to the four-stranded beta sheet and to the flexible loops on one end.

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Nature. 1990 Dec 6;348(6301):485-6.

PMID:: 2147232; [PubMed - indexed for MEDLINE]

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RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins. [Proc Natl Acad Sci U S A. 1991]
RNA-binding domain of the A protein component of the U1 small nuclear ribonucleoprotein analyzed by NMR spectroscopy is structurally similar to ribosomal proteins.
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Cited by over 100 PubMed Central articles

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Structures reported by this article

Sex-Lethal Rbd1, Nmr, Minimized Average Structure

PDB: 2SXL

Source: Drosophila melanogaster

Method: Solution Nmr

See all 4 structures...

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Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A.

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