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1ec6
From Proteopedia
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| - | [[Image:1ec6.gif|left|200px]] | + | [[Image:1ec6.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN''' | + | {{Structure |
| + | |PDB= 1ec6 |SIZE=350|CAPTION= <scene name='initialview01'>1ec6</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EC6 is a [ | + | 1EC6 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10676814 10676814] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rna-binding motif]] | [[Category: rna-binding motif]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:53:27 2008'' |
Revision as of 08:53, 20 March 2008
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| , resolution 2.40Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 10:53:27 2008
