1ie1

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(New page: 200px<br /><applet load="1ie1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ie1" /> '''NMR Solution Structure of an In Vitro Select...)
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'''NMR Solution Structure of an In Vitro Selected RNA which is Sequence Specifically Recognized by Hamster Nucleolin RBD12.'''<br />
'''NMR Solution Structure of an In Vitro Selected RNA which is Sequence Specifically Recognized by Hamster Nucleolin RBD12.'''<br />
==Overview==
==Overview==
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Nucleolin is an abundant nucleolar protein which is essential for ribosome, biogenesis. The first two of its four tandem RNA-binding domains (RBD12), specifically recognize a stem-loop structure containing a conserved UCCCGA, sequence in the loop called the nucleolin-recognition element (NRE). We, have determined the structure of the consensus SELEX NRE (sNRE) by NMR, spectroscopy. In both the free and bound RNA the top part of the stem, forms a loop E (or S-turn) motif. In the absence of protein, the structure, of the hairpin loop is not well defined due to conformational, heterogeneity, and appears to be in equilibrium between two families of, conformations. Titrations of RBD1, RBD2, and RBD12 with the sNRE show that, specific binding requires RBD12. In complex with RBD12, the hairpin loop, interacts specifically with the protein and adopts a well-defined, structure which shares some of the features of the free form. The loop E, motif also has specific interactions with the protein. Implications of, these findings for the mechanism of recognition of RNA structures by, modular proteins are discussed.
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Nucleolin is an abundant nucleolar protein which is essential for ribosome biogenesis. The first two of its four tandem RNA-binding domains (RBD12) specifically recognize a stem-loop structure containing a conserved UCCCGA sequence in the loop called the nucleolin-recognition element (NRE). We have determined the structure of the consensus SELEX NRE (sNRE) by NMR spectroscopy. In both the free and bound RNA the top part of the stem forms a loop E (or S-turn) motif. In the absence of protein, the structure of the hairpin loop is not well defined due to conformational heterogeneity, and appears to be in equilibrium between two families of conformations. Titrations of RBD1, RBD2, and RBD12 with the sNRE show that specific binding requires RBD12. In complex with RBD12, the hairpin loop interacts specifically with the protein and adopts a well-defined structure which shares some of the features of the free form. The loop E motif also has specific interactions with the protein. Implications of these findings for the mechanism of recognition of RNA structures by modular proteins are discussed.
==About this Structure==
==About this Structure==
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1IE1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IE1 OCA].
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1IE1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IE1 OCA].
==Reference==
==Reference==
Recognition of pre-formed and flexible elements of an RNA stem-loop by nucleolin., Bouvet P, Allain FH, Finger LD, Dieckmann T, Feigon J, J Mol Biol. 2001 Jun 8;309(3):763-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11397095 11397095]
Recognition of pre-formed and flexible elements of an RNA stem-loop by nucleolin., Bouvet P, Allain FH, Finger LD, Dieckmann T, Feigon J, J Mol Biol. 2001 Jun 8;309(3):763-75. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11397095 11397095]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Allain, F.H-T.]]
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[[Category: Allain, F H-T.]]
[[Category: Bouvet, P.]]
[[Category: Bouvet, P.]]
[[Category: Dieckmann, T.]]
[[Category: Dieckmann, T.]]
[[Category: Feigon, J.]]
[[Category: Feigon, J.]]
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[[Category: Finger, L.D.]]
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[[Category: Finger, L D.]]
[[Category: eucaryotic loop e motif a-form helix flexible loop]]
[[Category: eucaryotic loop e motif a-form helix flexible loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:51:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:55 2008''

Revision as of 11:10, 21 February 2008


1ie1

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NMR Solution Structure of an In Vitro Selected RNA which is Sequence Specifically Recognized by Hamster Nucleolin RBD12.

Overview

Nucleolin is an abundant nucleolar protein which is essential for ribosome biogenesis. The first two of its four tandem RNA-binding domains (RBD12) specifically recognize a stem-loop structure containing a conserved UCCCGA sequence in the loop called the nucleolin-recognition element (NRE). We have determined the structure of the consensus SELEX NRE (sNRE) by NMR spectroscopy. In both the free and bound RNA the top part of the stem forms a loop E (or S-turn) motif. In the absence of protein, the structure of the hairpin loop is not well defined due to conformational heterogeneity, and appears to be in equilibrium between two families of conformations. Titrations of RBD1, RBD2, and RBD12 with the sNRE show that specific binding requires RBD12. In complex with RBD12, the hairpin loop interacts specifically with the protein and adopts a well-defined structure which shares some of the features of the free form. The loop E motif also has specific interactions with the protein. Implications of these findings for the mechanism of recognition of RNA structures by modular proteins are discussed.

About this Structure

1IE1 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Recognition of pre-formed and flexible elements of an RNA stem-loop by nucleolin., Bouvet P, Allain FH, Finger LD, Dieckmann T, Feigon J, J Mol Biol. 2001 Jun 8;309(3):763-75. PMID:11397095

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