Journal Article

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

M. Sidiqi, J. A. Wilce, J. P. Vivian, C. J. Porter, A. Barker, P. J. Leedman and M. C. J. Wilce

in Nucleic Acids Research

Volume 33, issue 4, pages 1213-1221
Published in print February 2005 | ISSN: 0305-1048
Published online February 2005 | e-ISSN: 1362-4962 | DOI: https://dx.doi.org/10.1093/nar/gki265

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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 αCP1 to 2.1 Å resolution. αCP1-KH3 assumes a classical type I KH domain fold with a triple-stranded β-sheet held against a three-helix cluster in a βααββα 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 αCP1-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.

Journal Article.  6513 words.  Illustrated.

Subjects: Chemistry ; Biochemistry ; Bioinformatics and Computational Biology ; Genetics and Genomics ; Molecular and Cell Biology

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