1j75: Difference between revisions

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[[Image:1j75.gif|left|200px]]


{{Structure
==Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA==
|PDB= 1j75 |SIZE=350|CAPTION= <scene name='initialview01'>1j75</scene>, resolution 1.85&Aring;
<StructureSection load='1j75' size='340' side='right'caption='[[1j75]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
<table><tr><td colspan='2'>[[1j75]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J75 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j75 OCA], [https://pdbe.org/1j75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j75 RCSB], [https://www.ebi.ac.uk/pdbsum/1j75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j75 ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j75 OCA], [http://www.ebi.ac.uk/pdbsum/1j75 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j75 RCSB]</span>
[https://www.uniprot.org/uniprot/ZBP1_MOUSE ZBP1_MOUSE] Participates in the detection by the host's innate immune system of DNA from viral, bacterial or even host origin. Plays a role in host defense against tumors and pathogens. Acts as a cytoplasmic DNA sensor which, when activated, induces the recruitment of TBK1 and IRF3 to its C-terminal region and activates the downstream interferon regulatory factor (IRF) and NF-kappa B transcription factors, leading to type-I interferon production. ZBP1-induced NF-kappaB activation probably involves the recruitment of the RHIM containing kinases RIPK1 and RIPK3.<ref>PMID:17618271</ref> <ref>PMID:19590578</ref>
}}
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


'''Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA'''
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<ref>PMID:11524677</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1j75" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Z-DNA|Z-DNA]]
 
== References ==
==About this Structure==
<references/>
1J75 is a [[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].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11524677 11524677]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Behlke J]]
[[Category: Behlke, J.]]
[[Category: Heinemann U]]
[[Category: Heinemann, U.]]
[[Category: Lowenhaupt K]]
[[Category: Lowenhaupt, K.]]
[[Category: Rich A]]
[[Category: Rich, A.]]
[[Category: Schwartz T]]
[[Category: Schwartz, T.]]
[[Category: protein/z-dna complex]]
 
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