1j75: Difference between revisions

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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=''>
-{{ABSTRACT_PUBMED_11524677}}
+== 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>
+</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>
+</table>
+<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.
-==Function==
+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>
-[[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>
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[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].
+</div>
-==Reference==
+==See Also==
-<ref group="xtra">PMID:011524677</ref><references group="xtra"/><references/>
+*[[Z-DNA|Z-DNA]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[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]]