1wvn
From Proteopedia
(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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| - | [[Image:1wvn.gif|left|200px]]<br /> | + | [[Image:1wvn.gif|left|200px]]<br /><applet load="1wvn" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1wvn, resolution 2.10Å" /> | caption="1wvn, resolution 2.10Å" /> | ||
'''Crsytal Structure of domain 3 of human alpha polyC binding protein'''<br /> | '''Crsytal Structure of domain 3 of human alpha polyC binding protein'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Poly(C)-binding proteins (CPs) are important regulators of mRNA stability | + | 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== | ==About this Structure== | ||
| - | 1WVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1WVN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WVN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sidiqu, M.]] | [[Category: Sidiqu, M.]] | ||
| - | [[Category: Wilce, J | + | [[Category: Wilce, J A.]] |
| - | [[Category: Wilce, M | + | [[Category: Wilce, M C.J.]] |
[[Category: kh domain]] | [[Category: kh domain]] | ||
[[Category: rna binding domain]] | [[Category: rna binding domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:48:36 2008'' |
Revision as of 13:48, 21 February 2008
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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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