1ec6
From Proteopedia
(New page: 200px<br /> <applet load="1ec6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ec6, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...) |
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- | [[Image:1ec6.gif|left|200px]]<br /> | + | [[Image:1ec6.gif|left|200px]]<br /><applet load="1ec6" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1ec6" size=" | + | |
caption="1ec6, resolution 2.40Å" /> | caption="1ec6, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN'''<br /> | '''CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN'''<br /> | ||
==Overview== | ==Overview== | ||
- | The structure of a Nova protein K homology (KH) domain recognizing | + | The structure of a Nova protein K homology (KH) domain recognizing single-stranded RNA has been determined at 2.4 A resolution. Mammalian Nova antigens (1 and 2) constitute an important family of regulators of RNA metabolism in neurons, first identified using sera from cancer patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus ataxia (POMA). The structure of the third KH domain (KH3) of Nova-2 bound to a stem loop RNA resembles a molecular vise, with 5'-Ura-Cyt-Ade-Cyt-3' pinioned between an invariant Gly-X-X-Gly motif and the variable loop. Tetranucleotide recognition is supported by an aliphatic alpha helix/beta sheet RNA-binding platform, which mimics 5'-Ura-Gua-3' by making Watson-Crick-like hydrogen bonds with 5'-Cyt-Ade-3'. Sequence conservation suggests that fragile X mental retardation results from perturbation of RNA binding by the FMR1 protein. |
==About this Structure== | ==About this Structure== | ||
- | 1EC6 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:// | + | 1EC6 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=1EC6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen, H.]] | [[Category: Chen, H.]] | ||
[[Category: Edo, C.]] | [[Category: Edo, C.]] | ||
- | [[Category: Jensen, K | + | [[Category: Jensen, K B.]] |
- | [[Category: Lewis, H | + | [[Category: Lewis, H A.]] |
[[Category: Musunuru, K.]] | [[Category: Musunuru, K.]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
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[[Category: rna-binding motif]] | [[Category: rna-binding motif]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:10 2008'' |
Revision as of 10:26, 21 February 2008
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CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN
Overview
The structure of a Nova protein K homology (KH) domain recognizing single-stranded RNA has been determined at 2.4 A resolution. Mammalian Nova antigens (1 and 2) constitute an important family of regulators of RNA metabolism in neurons, first identified using sera from cancer patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus ataxia (POMA). The structure of the third KH domain (KH3) of Nova-2 bound to a stem loop RNA resembles a molecular vise, with 5'-Ura-Cyt-Ade-Cyt-3' pinioned between an invariant Gly-X-X-Gly motif and the variable loop. Tetranucleotide recognition is supported by an aliphatic alpha helix/beta sheet RNA-binding platform, which mimics 5'-Ura-Gua-3' by making Watson-Crick-like hydrogen bonds with 5'-Cyt-Ade-3'. Sequence conservation suggests that fragile X mental retardation results from perturbation of RNA binding by the FMR1 protein.
About this Structure
1EC6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome., Lewis HA, Musunuru K, Jensen KB, Edo C, Chen H, Darnell RB, Burley SK, Cell. 2000 Feb 4;100(3):323-32. PMID:10676814
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