1zzi

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(New page: 200px<br /> <applet load="1zzi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zzi, resolution 1.80&Aring;" /> '''Crystal Structure A...)
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caption="1zzi, resolution 1.80&Aring;" />
caption="1zzi, resolution 1.80&Aring;" />
'''Crystal Structure Analysis of the third KH domain of hnRNP K in complex with ssDNA'''<br />
'''Crystal Structure Analysis of the third KH domain of hnRNP K in complex with ssDNA'''<br />
==Overview==
==Overview==
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The heterogeneous nuclear ribonucleoprotein (hnRNP) K is implicated in, multiple functions in the regulation of gene expression and acts as a hub, at the intersection of signaling pathways and processes involving nucleic, acids. Central to its function is its ability to bind both ssDNA and ssRNA, via its KH (hnRNP K homology) domains. We determined crystal structures of, hnRNP K KH3 domain complexed with 15-mer and 6-mer (CTC(4)) ssDNAs at 2.4, and 1.8 A resolution, respectively, and show that the KH3 domain binds, specifically to both TCCC and CCCC sequences. In parallel, we used NMR to, compare the binding affinity and mode of interaction of the KH3 domain, with several ssRNA ligands and CTC(4) ssDNA. Based on a structure, alignment of the KH3-CTC(4) complex with known structures of other KH, domains in complex with ssRNA, we discuss recognition of tetranucleotide, sequences by KH domains.
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The heterogeneous nuclear ribonucleoprotein (hnRNP) K is implicated in multiple functions in the regulation of gene expression and acts as a hub at the intersection of signaling pathways and processes involving nucleic acids. Central to its function is its ability to bind both ssDNA and ssRNA via its KH (hnRNP K homology) domains. We determined crystal structures of hnRNP K KH3 domain complexed with 15-mer and 6-mer (CTC(4)) ssDNAs at 2.4 and 1.8 A resolution, respectively, and show that the KH3 domain binds specifically to both TCCC and CCCC sequences. In parallel, we used NMR to compare the binding affinity and mode of interaction of the KH3 domain with several ssRNA ligands and CTC(4) ssDNA. Based on a structure alignment of the KH3-CTC(4) complex with known structures of other KH domains in complex with ssRNA, we discuss recognition of tetranucleotide sequences by KH domains.
==About this Structure==
==About this Structure==
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1ZZI 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=1ZZI OCA].
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1ZZI 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=1ZZI OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Backe, P.H.]]
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[[Category: Backe, P H.]]
[[Category: Cusack, S.]]
[[Category: Cusack, S.]]
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[[Category: Messias, A.C.]]
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[[Category: Messias, A C.]]
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[[Category: Ravelli, R.B.]]
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[[Category: Ravelli, R B.]]
[[Category: Sattler, M.]]
[[Category: Sattler, M.]]
[[Category: protein-ssdna complex]]
[[Category: protein-ssdna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:43:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:40 2008''

Revision as of 14:20, 21 February 2008


1zzi, resolution 1.80Å

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Crystal Structure Analysis of the third KH domain of hnRNP K in complex with ssDNA

Overview

The heterogeneous nuclear ribonucleoprotein (hnRNP) K is implicated in multiple functions in the regulation of gene expression and acts as a hub at the intersection of signaling pathways and processes involving nucleic acids. Central to its function is its ability to bind both ssDNA and ssRNA via its KH (hnRNP K homology) domains. We determined crystal structures of hnRNP K KH3 domain complexed with 15-mer and 6-mer (CTC(4)) ssDNAs at 2.4 and 1.8 A resolution, respectively, and show that the KH3 domain binds specifically to both TCCC and CCCC sequences. In parallel, we used NMR to compare the binding affinity and mode of interaction of the KH3 domain with several ssRNA ligands and CTC(4) ssDNA. Based on a structure alignment of the KH3-CTC(4) complex with known structures of other KH domains in complex with ssRNA, we discuss recognition of tetranucleotide sequences by KH domains.

About this Structure

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

Reference

X-ray crystallographic and NMR studies of the third KH domain of hnRNP K in complex with single-stranded nucleic acids., Backe PH, Messias AC, Ravelli RB, Sattler M, Cusack S, Structure. 2005 Jul;13(7):1055-67. PMID:16004877

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