1wvn: Difference between revisions

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[[Image:1wvn.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1wvn|  PDB=1wvn  |  SCENE=  }}  
{{STRUCTURE_1wvn|  PDB=1wvn  |  SCENE=  }}  


'''Crsytal Structure of domain 3 of human alpha polyC binding protein'''
===Crsytal Structure of domain 3 of human alpha polyC binding protein===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Kh domain]]
[[Category: Kh domain]]
[[Category: Rna binding domain]]
[[Category: Rna binding domain]]
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Revision as of 18:21, 28 July 2008

File:1wvn.png

Template:STRUCTURE 1wvn

Crsytal Structure of domain 3 of human alpha polyC binding protein

Template:ABSTRACT PUBMED 15731341

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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