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| | ==Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA== | | ==Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA== |
| - | <StructureSection load='1j75' size='340' side='right' caption='[[1j75]], [[Resolution|resolution]] 1.85Å' scene=''> | + | <StructureSection load='1j75' size='340' side='right'caption='[[1j75]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1j75]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1J75 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1j75 RCSB], [http://www.ebi.ac.uk/pdbsum/1j75 PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| | + | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1j75" style="background-color:#fffaf0;"></div> |
| | | | |
| | ==See Also== | | ==See Also== |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[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: Immune system-dna complex]]
| + | |
| - | [[Category: Protein-z-dna complex]]
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| Structural highlights
Function
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.[1] [2]
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Takaoka A, Wang Z, Choi MK, Yanai H, Negishi H, Ban T, Lu Y, Miyagishi M, Kodama T, Honda K, Ohba Y, Taniguchi T. DAI (DLM-1/ZBP1) is a cytosolic DNA sensor and an activator of innate immune response. Nature. 2007 Jul 26;448(7152):501-5. Epub 2007 Jul 8. PMID:17618271 doi:http://dx.doi.org/10.1038/nature06013
- ↑ Rebsamen M, Heinz LX, Meylan E, Michallet MC, Schroder K, Hofmann K, Vazquez J, Benedict CA, Tschopp J. DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB. EMBO Rep. 2009 Aug;10(8):916-22. doi: 10.1038/embor.2009.109. Epub 2009 Jul 10. PMID:19590578 doi:http://dx.doi.org/10.1038/embor.2009.109
- ↑ Schwartz T, Behlke J, Lowenhaupt K, Heinemann U, Rich A. Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins. Nat Struct Biol. 2001 Sep;8(9):761-5. PMID:11524677 doi:10.1038/nsb0901-761
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