1nu4: Difference between revisions
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[[Image:1nu4.gif|left|200px]] | [[Image:1nu4.gif|left|200px]] | ||
'''U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix''' | {{Structure | ||
|PDB= 1nu4 |SIZE=350|CAPTION= <scene name='initialview01'>1nu4</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=MLA:MALONIC ACID'>MLA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''U1A RNA binding domain at 1.8 angstrom resolution reveals a pre-organized C-terminal helix''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NU4 is a [ | 1NU4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NU4 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12876372 12876372] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: u1 small nuclear ribonucleoprotein]] | [[Category: u1 small nuclear ribonucleoprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:01:41 2008'' | ||
Revision as of 11:01, 20 March 2008
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| 1nu4, resolution 1.80Å | |||||||||||||
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| Ligands: | MG and MLA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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