1WVN

Crystal Structure of domain 3 of human alpha polyC binding protein

Summary for 1WVN

• Entry DOI: 10.2210/pdb1wvn/pdb
• Descriptor: Poly(rC)-binding protein 1 (2 entities in total)
• Functional Keywords: kh domain, rna binding domain, rna binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8502.64

Authors

Wilce, M.C.J.,Wilce, J.A.,Sidiqu, M. (deposition date: 2004-12-17, release date: 2005-04-05, Last modification date: 2023-10-25)

Primary citation

Sidiqi, M.,Wilce, J.A.,Vivian, J.P.,Porter, C.J.,Barker, A.,Leedman, P.J.,Wilce, M.C.J.
Structure and RNA binding of the third KH domain of poly(C)-binding protein 1.
Nucleic Acids Res., 33:1213-1221, 2005

PubMed Abstract: 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.

PubMed: 15731341
DOI: 10.1093/nar/gki265

Experimental method

X-RAY DIFFRACTION (2.1 Å)