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Nucleic Acids Research 2005 33(4):1213-1221; doi:10.1093/nar/gki265
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Published online 24 February 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Structure and RNA binding of the third KH domain of poly(C)-binding protein 1

M. Sidiqi1, J. A. Wilce1, J. P. Vivian1,2, C. J. Porter1, A. Barker1,2, P. J. Leedman3,4 and M. C. J. Wilce1,2,4,*

1School of Biomedical and Chemical Sciences, the UWA Centre for Medical Research, The University of Western Australia WA Australia 6009 2School of Pharmacology and Medicine, the UWA Centre for Medical Research, The University of Western Australia WA Australia 6009 3Laboratory for Cancer Medicine, the UWA Centre for Medical Research, The University of Western Australia WA Australia 6009 4Western Australian Institute for Medical Research, The University of Western Australia WA Australia 6009

*To whom correspondence should be addressed at School of Pharmacology and Medicine and School of Biomedical and Chemical Sciences, University of Western Australia, 35 Stirling Highway, Crawley, Perth, Western Australia, 6009, Australia. Tel: +61 8 9346 2981; Fax: +61 8 9346 3469; Email: mwilce{at}receptor.pharm.uwa.edu.au

Received November 18, 2004. Revised January 12, 2005. Accepted February 3, 2005.

Poly(C)-binding proteins (CPs) are important regulators of mRNA stability and translational regulation. They recognize C-rich RNA through their triple KH (hn RNP K homology) domain structures and are thought to carry out their function though direct protection of mRNA sites as well as through interactions with other RNA-binding proteins. We report the crystallographically derived structure of the third domain of {alpha}CP1 to 2.1 Å resolution. {alpha}CP1-KH3 assumes a classical type I KH domain fold with a triple-stranded ß-sheet held against a three-helix cluster in a ß{alpha}{alpha}ßß{alpha} configuration. Its binding affinity to an RNA sequence from the 3'-untranslated region (3'-UTR) of androgen receptor mRNA was determined using surface plasmon resonance, giving a Kd of 4.37 µM, which is indicative of intermediate binding. A model of {alpha}CP1-KH3 with poly(C)-RNA was generated by homology to a recently reported RNA-bound KH domain structure and suggests the molecular basis for oligonucleotide binding and poly(C)-RNA specificity.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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