1j75: Difference between revisions

Latest revision as of 08:36, 16 August 2023

Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA

Structural highlights

1j75 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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:https://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:https://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

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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:https://dx.doi.org/10.1038/nature06013

[2] 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:https://dx.doi.org/10.1038/embor.2009.109

[3] 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

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
-[[Image:1j75.gif|left|200px]]
-<!--
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-You may change the PDB parameter (which sets the PDB file loaded into the applet)
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-{{STRUCTURE_1j75|  PDB=1j75  |  SCENE=  }}
-'''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]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<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='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>
+<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>
+== Function ==
+[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.
-==Overview==
+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>
-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==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-J75 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].
+</div>
+<div class="pdbe-citations 1j75" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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]
+*[[Z-DNA|Z-DNA]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[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]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:51:59 2008''

1j75: Difference between revisions

Latest revision as of 08:36, 16 August 2023

Crystal Structure of the DNA-Binding Domain Zalpha of DLM-1 Bound to Z-DNA

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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