1j5k

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(New page: 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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<applet load="1j5k" size="450" color="white" frame="true" align="right" spinBox="true"
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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==
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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.
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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==
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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].
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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]]
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[[Category: Braddock, D.T.]]
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[[Category: Braddock, D T.]]
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[[Category: Clore, G.M.]]
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[[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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:37:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:07 2008''

Revision as of 11:19, 21 February 2008


1j5k

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COMPLEX OF THE KH3 DOMAIN OF HNRNP K WITH A SINGLE_STRANDED 10MER DNA OLIGONUCLEOTIDE

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.

About this Structure

1J5K is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA., Braddock DT, Baber JL, Levens D, Clore GM, EMBO J. 2002 Jul 1;21(13):3476-85. PMID:12093748

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