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1rkj

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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'''
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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===
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15033352 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15033352}}
==About this Structure==
==About this Structure==
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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].
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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].
==Reference==
==Reference==
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[[Category: Protein-rna complex]]
[[Category: Protein-rna complex]]
[[Category: Rbd]]
[[Category: Rbd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:36:38 2008''
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''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

Image:1rkj.png

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

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