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New page: left|200px<br /><applet load="2cjk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cjk" /> '''STRUCTURE OF THE RNA BINDING DOMAIN OF HRP1 ...
 
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[[Image:2cjk.jpg|left|200px]]<br /><applet load="2cjk" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2cjk.jpg|left|200px]]<br /><applet load="2cjk" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2cjk" />
caption="2cjk" />
'''STRUCTURE OF THE RNA BINDING DOMAIN OF HRP1 IN COMPLEX WITH RNA'''<br />
'''STRUCTURE OF THE RNA BINDING DOMAIN OF HRP1 IN COMPLEX WITH RNA'''<br />


==Overview==
==Overview==
The recognition of specific signals encoded within the 3'-untranslated, region of the newly transcribed mRNA triggers the assembly of a, multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such, signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The, molecular bases of this interaction are revealed here by the solution, structure of a complex between Hrp1 and an oligonucleotide mimicking the, PEE. Six consecutive bases (AUAUAU) are specifically recognised by two, RNA-binding domains arranged in tandem. Both protein and RNA undergo, significant conformational changes upon complex formation with a, concomitant large surface burial of RNA bases. Key aspects of RNA, specificity can be explained by the presence of intermolecular, aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE, structure represents one of the first steps towards understanding of the, assembly of the cleavage and polyadenylation machinery at the atomic, level.
The recognition of specific signals encoded within the 3'-untranslated region of the newly transcribed mRNA triggers the assembly of a multiprotein machine that modifies its 3'-end. Hrp1 recognises one of such signals, the so-called polyadenylation enhancement element (PEE), promoting the recruitment of other polyadenylation factors in yeast. The molecular bases of this interaction are revealed here by the solution structure of a complex between Hrp1 and an oligonucleotide mimicking the PEE. Six consecutive bases (AUAUAU) are specifically recognised by two RNA-binding domains arranged in tandem. Both protein and RNA undergo significant conformational changes upon complex formation with a concomitant large surface burial of RNA bases. Key aspects of RNA specificity can be explained by the presence of intermolecular aromatic-aromatic contacts and hydrogen bonds. Altogether, the Hrp1-PEE structure represents one of the first steps towards understanding of the assembly of the cleavage and polyadenylation machinery at the atomic level.


==About this Structure==
==About this Structure==
2CJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CJK OCA].  
2CJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJK OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Perez-Canadillas, J.M.]]
[[Category: Perez-Canadillas, J M.]]
[[Category: cleavage]]
[[Category: cleavage]]
[[Category: hrp1]]
[[Category: hrp1]]
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[[Category: rna-binding protein]]
[[Category: rna-binding protein]]


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