From Proteopedia
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| | {{STRUCTURE_1rkj| PDB=1rkj | SCENE= }} | | {{STRUCTURE_1rkj| PDB=1rkj | SCENE= }} |
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| - | '''Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target'''
| + | ===Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target=== |
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| - | ==Overview==
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| - | Nucleolin is a 70 kDa multidomain protein involved in several steps of eukaryotic ribosome biogenesis. In vitro selection in combination with mutagenesis and structural analysis identified binding sites in pre-rRNA with the consensus (U/G)CCCG(A/G) in the context of a hairpin structure, the nucleolin recognition element (NRE). The central region of the protein contains four tandem RNA-binding domains (RBDs), of which the first two are responsible for the RNA-binding specificity and affinity for NREs. Here, we present the solution structure of the 28 kDa complex formed by the two N-terminal RNA-binding domains of nucleolin (RBD12) and a natural pre-rRNA target, b2NRE. The structure demonstrates that the sequence-specific recognition of the pre-rRNA NRE is achieved by intermolecular hydrogen bonds and stacking interactions involving mainly the beta-sheet surfaces of the two RBDs and the linker residues. A comparison with our previously determined NMR structure of RBD12 in complex with an in vitro selected RNA target, sNRE, shows that although the sequence-specific recognition of the loop consensus nucleotides is the same in the two complexes, they differ in several aspects. While the protein makes numerous specific contacts to the non-consensus nucleotides in the loop E motif (S-turn) in the upper part of the sNRE stem, nucleolin RBD12 contacts only consensus nucleotides in b2NRE. The absence of these upper stem contacts from the RBD12/b2NRE complex results in a much less stable complex, as demonstrated by kinetic analyses. The role of the loop E motif in high-affinity binding is supported by gel-shift analyses with a series of sNRE mutants. The less stable interaction of RBD12 with the natural RNA target is consistent with the proposed role of nucleolin as a chaperone that interacts transiently with pre-rRNA to prevent misfolding.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15033352}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15033352 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15033352}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1RKJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKJ OCA]. | + | 1RKJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKJ OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Protein-rna complex]] | | [[Category: Protein-rna complex]] |
| | [[Category: Rbd]] | | [[Category: Rbd]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:36:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:35:27 2008'' |
Revision as of 05:35, 28 July 2008
Template:STRUCTURE 1rkj
Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target
Template:ABSTRACT PUBMED 15033352
About this Structure
1RKJ is a Single protein structure of sequence from Mesocricetus auratus. Full experimental information is available from OCA.
Reference
Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target., Johansson C, Finger LD, Trantirek L, Mueller TD, Kim S, Laird-Offringa IA, Feigon J, J Mol Biol. 2004 Apr 2;337(4):799-816. PMID:15033352
Page seeded by OCA on Mon Jul 28 08:35:27 2008
