1qu6

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[[Image:1qu6.jpg|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qu6 OCA], [http://www.ebi.ac.uk/pdbsum/1qu6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qu6 RCSB]</span>
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'''STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED ACTIVATION'''
'''STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED ACTIVATION'''
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[[Category: Williams, B R.G.]]
[[Category: Williams, B R.G.]]
[[Category: Yang, Y.]]
[[Category: Yang, Y.]]
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[[Category: dsrna-binding domain]]
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[[Category: Dsrna-binding domain]]
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[[Category: nmr]]
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[[Category: Nmr]]
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[[Category: pkr]]
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[[Category: Pkr]]
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[[Category: protein kinase]]
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[[Category: Protein kinase]]
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[[Category: solution structure]]
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[[Category: Solution structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:42:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:09 2008''
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Revision as of 03:42, 3 May 2008

Template:STRUCTURE 1qu6

STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED ACTIVATION


Overview

Protein kinase PKR is an interferon-induced enzyme that plays a key role in the control of viral infections and cellular homeostasis. Compared with other known kinases, PKR is activated by a distinct mechanism that involves double-stranded RNA (dsRNA) binding in its N-terminal region in an RNA sequence-independent fashion. We report here the solution structure of the 20 kDa dsRNA-binding domain (dsRBD) of human PKR, which provides the first three-dimensional insight into the mechanism of its dsRNA-mediated activation. The structure of dsRBD exhibits a dumb-bell shape comprising two tandem linked dsRNA-binding motifs (dsRBMs) both with an alpha-beta-beta-beta-alpha fold. The structure, combined with previous mutational and biochemical data, reveals a highly conserved RNA-binding site on each dsRBM and suggests a novel mode of protein-RNA recognition. The central linker is highly flexible, which may enable the two dsRBMs to wrap around the RNA duplex for cooperative and high-affinity binding, leading to the overall change of PKR conformation and its activation.

About this Structure

1QU6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation., Nanduri S, Carpick BW, Yang Y, Williams BR, Qin J, EMBO J. 1998 Sep 15;17(18):5458-65. PMID:9736623 Page seeded by OCA on Sat May 3 06:42:34 2008

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