1di2: Difference between revisions

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[[Image:1di2.jpg|left|200px]]
[[Image:1di2.jpg|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1di2 OCA], [http://www.ebi.ac.uk/pdbsum/1di2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1di2 RCSB]</span>
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'''CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS'''
'''CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS'''
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[[Category: Ryter, J M.]]
[[Category: Ryter, J M.]]
[[Category: Schultz, S C.]]
[[Category: Schultz, S C.]]
[[Category: double stranded rna]]
[[Category: Double stranded rna]]
[[Category: protein-rna complex]]
[[Category: Protein-rna complex]]
[[Category: protein-rna interaction]]
[[Category: Protein-rna interaction]]
[[Category: rna-bining protein]]
[[Category: Rna-bining protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:41:56 2008''

Revision as of 10:51, 2 May 2008

File:1di2.jpg

Template:STRUCTURE 1di2

CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS


Overview

Protein interactions with double-stranded RNA (dsRNA) are critical for many cell processes; however, in contrast to protein-dsDNA interactions, surprisingly little is known about the molecular basis of protein-dsRNA interactions. A large and diverse class of proteins that bind dsRNA do so by utilizing an approximately 70 amino acid motif referred to as the dsRNA-binding domain (dsRBD). We have determined a 1.9 A resolution crystal structure of the second dsRBD of Xenopus laevis RNA-binding protein A complexed with dsRNA. The structure shows that the protein spans 16 bp of dsRNA, interacting with two successive minor grooves and across the intervening major groove on one face of a primarily A-form RNA helix. The nature of these interactions explains dsRBD specificity for dsRNA (over ssRNA or dsDNA) and the apparent lack of sequence specificity. Interestingly, the dsRBD fold resembles a portion of the conserved core structure of a family of polynucleotidyl transferases that includes RuvC, MuA transposase, retroviral integrase and RNase H. Structural comparisons of the dsRBD-dsRNA complex and models proposed for polynucleotidyl transferase-nucleic acid complexes suggest that similarities in nucleic acid binding also exist between these families of proteins.

About this Structure

1DI2 is a Single protein structure of sequence from Xenopus laevis. Full crystallographic information is available from OCA.

Reference

Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA., Ryter JM, Schultz SC, EMBO J. 1998 Dec 15;17(24):7505-13. PMID:9857205 Page seeded by OCA on Fri May 2 13:51:55 2008

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