1s79

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'''Solution structure of the central RRM of human La protein'''<br />
'''Solution structure of the central RRM of human La protein'''<br />
==Overview==
==Overview==
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The La protein is a conserved component of eukaryotic ribonucleoprotein, complexes that binds the 3' poly(U)-rich elements of nascent RNA, polymerase III (pol III) transcripts to assist folding and maturation., This specific recognition is mediated by the N-terminal domain (NTD) of, La, which comprises a La motif and an RNA recognition motif (RRM). We have, determined the solution structures of both domains and show that the La, motif adopts an alpha/beta fold that comprises a winged-helix motif, elaborated by the insertion of three helices. Chemical shift mapping, experiments show that these insertions are involved in RNA interactions., They further delineate a distinct surface patch on each domain-containing, both basic and aromatic residues-that interacts with RNA and accounts for, the cooperative binding of short oligonucleotides exhibited by the La NTD.
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The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3' poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). We have determined the solution structures of both domains and show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions. They further delineate a distinct surface patch on each domain-containing both basic and aromatic residues-that interacts with RNA and accounts for the cooperative binding of short oligonucleotides exhibited by the La NTD.
==About this Structure==
==About this Structure==
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1S79 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S79 OCA].
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1S79 is a [http://en.wikipedia.org/wiki/Single_protein 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=1S79 OCA].
==Reference==
==Reference==
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[[Category: Alfano, C.]]
[[Category: Alfano, C.]]
[[Category: Babon, J.]]
[[Category: Babon, J.]]
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[[Category: Conte, M.R.]]
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[[Category: Conte, M R.]]
[[Category: Curry, S.]]
[[Category: Curry, S.]]
[[Category: Jacks, A.]]
[[Category: Jacks, A.]]
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[[Category: rrm]]
[[Category: rrm]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:11:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:58:44 2008''

Revision as of 12:58, 21 February 2008

Image:1s79.gif

1s79

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Solution structure of the central RRM of human La protein

Overview

The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3' poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). We have determined the solution structures of both domains and show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions. They further delineate a distinct surface patch on each domain-containing both basic and aromatic residues-that interacts with RNA and accounts for the cooperative binding of short oligonucleotides exhibited by the La NTD.

About this Structure

1S79 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein., Alfano C, Sanfelice D, Babon J, Kelly G, Jacks A, Curry S, Conte MR, Nat Struct Mol Biol. 2004 Apr;11(4):323-9. Epub 2004 Mar 7. PMID:15004549

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