1j75
From Proteopedia
(New page: 200px<br /><applet load="1j75" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j75, resolution 1.85Å" /> '''Crystal Structure of...) |
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| - | [[Image:1j75.gif|left|200px]]<br /><applet load="1j75" size=" | + | [[Image:1j75.gif|left|200px]]<br /><applet load="1j75" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1j75, resolution 1.85Å" /> | caption="1j75, resolution 1.85Å" /> | ||
'''Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA'''<br /> | '''Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The first crystal structure of a protein, the Z alpha high affinity | + | The first crystal structure of a protein, the Z alpha high affinity binding domain of the RNA editing enzyme ADAR1, bound to left-handed Z-DNA was recently described. The essential set of residues determined from this structure to be critical for Z-DNA recognition was used to search the database for other proteins with the potential for Z-DNA binding. We found that the tumor-associated protein DLM-1 contains a domain with remarkable sequence similarities to Z alpha(ADAR). Here we report the crystal structure of this DLM-1 domain bound to left-handed Z-DNA at 1.85 A resolution. Comparison of Z-DNA binding by DLM-1 and ADAR1 reveals a common structure-specific recognition core within the binding domain. However, the domains differ in certain residues peripheral to the protein-DNA interface. These structures reveal a general mechanism of Z-DNA recognition, suggesting the existence of a family of winged-helix proteins sharing a common Z-DNA binding motif. |
==About this Structure== | ==About this Structure== | ||
| - | 1J75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1J75 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J75 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein/z-dna complex]] | [[Category: protein/z-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:24 2008'' |
Revision as of 11:19, 21 February 2008
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Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA
Overview
The first crystal structure of a protein, the Z alpha high affinity binding domain of the RNA editing enzyme ADAR1, bound to left-handed Z-DNA was recently described. The essential set of residues determined from this structure to be critical for Z-DNA recognition was used to search the database for other proteins with the potential for Z-DNA binding. We found that the tumor-associated protein DLM-1 contains a domain with remarkable sequence similarities to Z alpha(ADAR). Here we report the crystal structure of this DLM-1 domain bound to left-handed Z-DNA at 1.85 A resolution. Comparison of Z-DNA binding by DLM-1 and ADAR1 reveals a common structure-specific recognition core within the binding domain. However, the domains differ in certain residues peripheral to the protein-DNA interface. These structures reveal a general mechanism of Z-DNA recognition, suggesting the existence of a family of winged-helix proteins sharing a common Z-DNA binding motif.
About this Structure
1J75 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins., Schwartz T, Behlke J, Lowenhaupt K, Heinemann U, Rich A, Nat Struct Biol. 2001 Sep;8(9):761-5. PMID:11524677
Page seeded by OCA on Thu Feb 21 13:19:24 2008
