1di2

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|PDB= 1di2 |SIZE=350|CAPTION= <scene name='initialview01'>1di2</scene>, resolution 1.90&Aring;
|PDB= 1di2 |SIZE=350|CAPTION= <scene name='initialview01'>1di2</scene>, resolution 1.90&Aring;
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|LIGAND= <scene name='pdbligand=C:CYTIDINE-5&#39;-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5&#39;-MONOPHOSPHATE'>G</scene>
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|ACTIVITY=
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|DOMAIN=
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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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[[Category: rna-bining protein]]
[[Category: rna-bining protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:38:40 2008''
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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 16:41, 30 March 2008


PDB ID 1di2

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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