1ec6

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(New page: 200px<br /> <applet load="1ec6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ec6, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
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caption="1ec6, resolution 2.40&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EC6 OCA].
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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.]]
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[[Category: Jensen, K.B.]]
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[[Category: Jensen, K B.]]
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[[Category: Lewis, H.A.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:42:03 2007''
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''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


1ec6, resolution 2.40Å

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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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