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Publication Abstract from PubMed

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 alphaCP1 to 2.1 A resolution. alphaCP1-KH3 assumes a classical type I KH domain fold with a triple-stranded beta-sheet held against a three-helix cluster in a betaalphaalphabetabetaalpha 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 K(d) of 4.37 microM, which is indicative of intermediate binding. A model of alphaCP1-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.

Structure and RNA binding of the third KH domain of poly(C)-binding protein 1.,Sidiqi M, Wilce JA, Vivian JP, Porter CJ, Barker A, Leedman PJ, Wilce MC Nucleic Acids Res. 2005 Feb 24;33(4):1213-21. Print 2005. PMID:15731341^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.