From Proteopedia
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| | {{STRUCTURE_1dt4| PDB=1dt4 | SCENE= }} | | {{STRUCTURE_1dt4| PDB=1dt4 | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN'''
| + | ===CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN=== |
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| - | ==Overview==
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| - | BACKGROUND: Nova-1 and Nova-2 are related neuronal proteins that were initially cloned using antisera obtained from patients with the autoimmune neurological disease paraneoplastic opsoclonus-myoclonus ataxia (POMA). Both of these disease gene products contain three RNA-binding motifs known as K-homology or KH domains, and their RNA ligands have been identified via binding-site selection experiments. The KH motif structure has been determined previously using NMR spectroscopy, but not using X-ray crystallography. Many proteins contain more than one KH domain, yet there is no published structural information regarding the behavior of such multimers. RESULTS: We have obtained the first X-ray crystallographic structures of KH-domain-containing proteins. Structures of the third KH domains (KH3) of Nova-1 and Nova-2 were determined by multiple isomorphous replacement and molecular replacement at 2.6 A and 2.0 A, respectively. These highly similar RNA-binding motifs form a compact protease-resistant domain resembling an open-faced sandwich, consisting of a three-stranded antiparallel beta sheet topped by three alpha helices. In both Nova crystals, the lattice is composed of symmetric tetramers of KH3 domains that are created by two dimer interfaces. CONCLUSIONS: The crystal structures of both Nova KH3 domains are similar to the previously determined NMR structures. The most significant differences among the KH domains involve changes in the positioning of one or more of the alpha helices with respect to the betasheet, particularly in the NMR structure of the KH1 domain of the Fragile X disease protein FMR-1. Loop regions in the KH domains are clearly visible in the crystal structure, unlike the NMR structures, revealing the conformation of the invariant Gly-X-X-Gly segment that is thought to participate in RNA-binding and of the variable region. The tetrameric arrangements of the Nova KH3 domains provide insights into how KH domains may interact with each other in proteins containing multiple KH motifs.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10368286}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10368286 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10368286}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Kh domain]] | | [[Category: Kh domain]] |
| | [[Category: Rna-binding motif]] | | [[Category: Rna-binding motif]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:14:37 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:34:46 2008'' |
Revision as of 20:34, 30 June 2008
Template:STRUCTURE 1dt4
CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN
Template:ABSTRACT PUBMED 10368286
About this Structure
1DT4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains., Lewis HA, Chen H, Edo C, Buckanovich RJ, Yang YY, Musunuru K, Zhong R, Darnell RB, Burley SK, Structure. 1999 Feb 15;7(2):191-203. PMID:10368286
Page seeded by OCA on Mon Jun 30 23:34:46 2008
