1rkj

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[[Image:1rkj.gif|left|200px]]<br /><applet load="1rkj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rkj.gif|left|200px]]
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caption="1rkj" />
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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'''<br />
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{{Structure
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|PDB= 1rkj |SIZE=350|CAPTION= <scene name='initialview01'>1rkj</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= NCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10036 Mesocricetus auratus])
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}}
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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==
==Overview==
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==About this Structure==
==About this Structure==
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1RKJ is a [http://en.wikipedia.org/wiki/Single_protein 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKJ OCA].
==Reference==
==Reference==
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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., 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15033352 15033352]
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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., 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:[http://www.ncbi.nlm.nih.gov/pubmed/15033352 15033352]
[[Category: Mesocricetus auratus]]
[[Category: Mesocricetus auratus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rbd]]
[[Category: rbd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:51:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:52:51 2008''

Revision as of 11:52, 20 March 2008


PDB ID 1rkj

Drag the structure with the mouse to rotate
Gene: NCL (Mesocricetus auratus)
Coordinates: save as pdb, mmCIF, xml



Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target


Overview

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.

About this Structure

1RKJ is a Single protein structure of sequence from Mesocricetus auratus. Full crystallographic 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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