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1wvn
From Proteopedia
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'''Crsytal Structure of domain 3 of human alpha polyC binding protein''' | '''Crsytal Structure of domain 3 of human alpha polyC binding protein''' | ||
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[[Category: Wilce, J A.]] | [[Category: Wilce, J A.]] | ||
[[Category: Wilce, M C.J.]] | [[Category: Wilce, M C.J.]] | ||
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Revision as of 11:12, 3 May 2008
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 Page seeded by OCA on Sat May 3 14:12:01 2008
