1wvn
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(New page: 200px<br /> <applet load="1wvn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wvn, resolution 2.10Å" /> '''Crsytal Structure o...)
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Revision as of 17:48, 12 November 2007
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Crsytal Structure of domain 3 of human alpha polyC binding protein
Overview
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.
About this Structure
1WVN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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