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, Andrew Barker, Peter Leedman, M.C.J. Wilce

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Poly(C)-binding proteins (CPs) are important regulators of mRNA stability and translational regulation. They recognize C-richRNA 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 angstrom resolution. alpha CP1-KH3 assumes a classical type I KH domain fold with a triple-stranded beta-sheet held against a three-helix cluster in a beta alpha alpha beta beta 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 K-d of 4.37 mu M, 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.
Original languageEnglish
Pages (from-to)1213-1221
JournalNucleic Acids Research
Volume33
Issue number4
DOIs
Publication statusPublished - 2005

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