1zzk
From Proteopedia
(New page: 200px<br /> <applet load="1zzk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zzk, resolution 0.95Å" /> '''Crystal Structure o...) |
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| - | [[Image:1zzk.gif|left|200px]]<br /> | + | [[Image:1zzk.gif|left|200px]]<br /><applet load="1zzk" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1zzk, resolution 0.95Å" /> | caption="1zzk, resolution 0.95Å" /> | ||
'''Crystal Structure of the third KH domain of hnRNP K at 0.95A resolution'''<br /> | '''Crystal Structure of the third KH domain of hnRNP K at 0.95A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The heterogeneous nuclear ribonucleoprotein (hnRNP) K is implicated in | + | 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== | ||
| - | 1ZZK 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:// | + | 1ZZK 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=1ZZK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Backe, P | + | [[Category: Backe, P H.]] |
[[Category: Cusack, S.]] | [[Category: Cusack, S.]] | ||
| - | [[Category: Messias, A | + | [[Category: Messias, A C.]] |
| - | [[Category: Ravelli, R | + | [[Category: Ravelli, R B.]] |
[[Category: Sattler, M.]] | [[Category: Sattler, M.]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
[[Category: kh domian]] | [[Category: kh domian]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:36 2008'' |
Revision as of 14:20, 21 February 2008
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Crystal Structure of the third KH domain of hnRNP K at 0.95A resolution
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
1ZZK 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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