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1nu4

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nu4 OCA], [http://www.ebi.ac.uk/pdbsum/1nu4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nu4 RCSB]</span>
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'''U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix'''
'''U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix'''
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[[Category: Rupert, P B.]]
[[Category: Rupert, P B.]]
[[Category: Xiao, H.]]
[[Category: Xiao, H.]]
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[[Category: rna binding domain]]
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[[Category: Rna binding domain]]
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[[Category: rna recognition motif]]
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[[Category: Rna recognition motif]]
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[[Category: u1 small nuclear ribonucleoprotein]]
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[[Category: U1 small nuclear ribonucleoprotein]]
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Revision as of 23:58, 2 May 2008

Template:STRUCTURE 1nu4

U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix


Overview

The human U1A RNA-binding domain (RBD1) adopts one of the most common protein folds, the RNA-recognition motif, and is a paradigm for understanding RNA-protein interactions. A 2.8 A resolution structure of the unbound RBD1 has previously been determined [Nagai et al. (1990). Nature (London), 348, 515-520] and revealed a well defined alpha/beta core with disordered termini. Using a longer construct, a 1.8 A resolution structure of the unbound domain was determined that reveals an ordered C-terminal helix. The presence of this helix is consistent with a solution structure of the free domain [Avis et al. (1996). J. Mol. Biol. 257, 398-411]; however, in the solution structure the helix occludes the RNA-binding surface. In the present structure, the helix occupies a position similar to that seen in a 1.9 A resolution RNA-RBD1 complex structure [Oubridge et al. (1994). Nature (London), 372, 432-438]. The crystals in this study were grown from 2.2 M sodium malonate. It is possible that the high salt concentration helps to orient the C-terminal helix in the RNA-bound conformation by strengthening hydrophobic interactions between the buried face of the helix and the alpha/beta core of the protein. Alternatively, the malonate (several molecules of which are bound in the vicinity of the RNA-binding surface) may mimic RNA.

About this Structure

1NU4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

U1A RNA-binding domain at 1.8 A resolution., Rupert PB, Xiao H, Ferre-D'Amare AR, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1521-4. Epub 2003, Jul 23. PMID:12876372 Page seeded by OCA on Sat May 3 02:58:50 2008

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