1di2: Difference between revisions
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'''CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS''' | {{Structure | ||
|PDB= 1di2 |SIZE=350|CAPTION= <scene name='initialview01'>1di2</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DI2 is a [ | 1DI2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI2 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9857205 9857205] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: double stranded rna]] | [[Category: double stranded rna]] | ||
[[Category: protein-rna complex]] | [[Category: protein-rna complex]] | ||
[[Category: protein-rna | [[Category: protein-rna interaction]] | ||
[[Category: rna-bining protein]] | [[Category: rna-bining protein]] | ||
''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 10:38:40 2008'' | ||
Revision as of 08:38, 20 March 2008
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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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