1nu4
From Proteopedia
(New page: 200px<br /> <applet load="1nu4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nu4, resolution 1.80Å" /> '''U1A RNA binding dom...) |
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| - | [[Image:1nu4.gif|left|200px]]<br /> | + | [[Image:1nu4.gif|left|200px]]<br /><applet load="1nu4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nu4" size=" | + | |
caption="1nu4, resolution 1.80Å" /> | caption="1nu4, resolution 1.80Å" /> | ||
'''U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix'''<br /> | '''U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human U1A RNA-binding domain (RBD1) adopts one of the most common | + | 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== | ==About this Structure== | ||
| - | 1NU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and MLA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NU4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=MLA:'>MLA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amare, A | + | [[Category: Amare, A R.Ferre-D.]] |
| - | [[Category: Rupert, P | + | [[Category: Rupert, P B.]] |
[[Category: Xiao, H.]] | [[Category: Xiao, H.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: u1 small nuclear ribonucleoprotein]] | [[Category: u1 small nuclear ribonucleoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:00 2008'' |
Revision as of 12:10, 21 February 2008
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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 with and as ligands. 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
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