1j5k: Difference between revisions

New page: left|200px<br /> <applet load="1j5k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j5k" /> '''COMPLEX OF THE KH3 DOMAIN OF HNRNP K WITH A...
 
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[[Image:1j5k.gif|left|200px]]<br /><applet load="1j5k" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1j5k" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1j5k" />
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'''COMPLEX OF THE KH3 DOMAIN OF HNRNP K WITH A SINGLE_STRANDED 10MER DNA OLIGONUCLEOTIDE'''<br />
'''COMPLEX OF THE KH3 DOMAIN OF HNRNP K WITH A SINGLE_STRANDED 10MER DNA OLIGONUCLEOTIDE'''<br />


==Overview==
==Overview==
To elucidate the basis of sequence-specific single-stranded (ss) DNA, recognition by K homology (KH) domains, we have solved the solution, structure of a complex between the KH3 domain of the transcriptional, regulator heterogeneous nuclear ribonucleoprotein K (hnRNP K) and a 10mer, ssDNA. We show that hnRNP K KH3 specifically recognizes a tetrad of, sequence 5'd-TCCC. The complex is stabilized by a dense network of, methyl-oxygen hydrogen bonds involving the methyl groups of three, isoleucine residues and the O2 and N3 atoms of the two central cytosine, bases. Comparison with the recently solved structure of a specific, protein-ssDNA complex involving the KH3 and KH4 domains of the far, upstream element (FUSE) binding protein FBP suggests that the amino acid, located five residues N-terminal of the invariant GXXG motif, which is, characteristic of all KH domains, plays a crucial role in discrimination, of the first two bases of the tetrad.
To elucidate the basis of sequence-specific single-stranded (ss) DNA recognition by K homology (KH) domains, we have solved the solution structure of a complex between the KH3 domain of the transcriptional regulator heterogeneous nuclear ribonucleoprotein K (hnRNP K) and a 10mer ssDNA. We show that hnRNP K KH3 specifically recognizes a tetrad of sequence 5'd-TCCC. The complex is stabilized by a dense network of methyl-oxygen hydrogen bonds involving the methyl groups of three isoleucine residues and the O2 and N3 atoms of the two central cytosine bases. Comparison with the recently solved structure of a specific protein-ssDNA complex involving the KH3 and KH4 domains of the far upstream element (FUSE) binding protein FBP suggests that the amino acid located five residues N-terminal of the invariant GXXG motif, which is characteristic of all KH domains, plays a crucial role in discrimination of the first two bases of the tetrad.


==About this Structure==
==About this Structure==
1J5K 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J5K OCA].  
1J5K 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=1J5K OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Braddock, D.T.]]
[[Category: Braddock, D T.]]
[[Category: Clore, G.M.]]
[[Category: Clore, G M.]]
[[Category: c-myc oncogene]]
[[Category: c-myc oncogene]]
[[Category: ct element]]
[[Category: ct element]]
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[[Category: transcription factor]]
[[Category: transcription factor]]


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