2ci6: Difference between revisions

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-{{Seed}}
-[[Image:2ci6.png|left|200px]]
-<!--
+==Crystal Structure of Dimethylarginine dimethylaminohydrolase I bound with Zinc low pH==
-The line below this paragraph, containing "STRUCTURE_2ci6", creates the "Structure Box" on the page.
+<StructureSection load='2ci6' size='340' side='right'caption='[[2ci6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ci6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CI6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_2ci6|  PDB=2ci6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ci6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ci6 OCA], [https://pdbe.org/2ci6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ci6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ci6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ci6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DDAH1_BOVIN DDAH1_BOVIN] Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ci/2ci6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ci6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Dimethylarginine dimethylaminohydrolase (DDAH) is involved in the regulation of nitric oxide synthase (NOS) by metabolizing the free endogenous arginine derivatives N(omega)-methyl-L-arginine (MMA) and N(omega),N(omega)-dimethyl-L-arginine (ADMA), which are competitive inhibitors of NOS. Here, we present high-resolution crystal structures of DDAH isoform 1 (DDAH-1) isolated from bovine brain in complex with different inhibitors, including S-nitroso-L-homocysteine and Zn2+, a regulator of this mammalian enzyme. The structure of DDAH-1 consists of a propeller-like fold similar to other arginine-modifying enzymes and a flexible loop, which adopts different conformations and acts as a lid at the entrance of the active site. The orientation and interaction mode of inhibitors in the active site give insight into the regulation and the molecular mechanism of the enzyme. The presented structures provide a basis for the structure-based development of specific DDAH-1 inhibitors that might be useful in the therapeutic treatment of NOS dysfunction-related diseases.
-===CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I BOUND WITH ZINC LOW PH===
+Structure of the mammalian NOS regulator dimethylarginine dimethylaminohydrolase: A basis for the design of specific inhibitors.,Frey D, Braun O, Briand C, Vasak M, Grutter MG Structure. 2006 May;14(5):901-11. PMID:16698551<ref>PMID:16698551</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16698551}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2ci6" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16698551 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16698551}}
+__TOC__
+</StructureSection>
-==About this Structure==
-CI6 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI6 OCA].
-==Reference==
-<ref group="xtra">PMID:16698551</ref><references group="xtra"/>
 [[Category: Bos taurus]]
-[[Category: Dimethylargininase]]
+[[Category: Large Structures]]
-[[Category: Braun, O.]]
+[[Category: Braun O]]
-[[Category: Briand, C.]]
+[[Category: Briand C]]
-[[Category: Frey, D.]]
+[[Category: Frey D]]
-[[Category: Grutter, M G.]]
+[[Category: Grutter MG]]
-[[Category: Vasak, M.]]
+[[Category: Vasak M]]
-[[Category: Acetylation]]
-[[Category: Adma]]
-[[Category: Hydrolase]]
-[[Category: Metal-binding]]
-[[Category: Mma]]
-[[Category: No]]
-[[Category: Nos regulation]]
-[[Category: S-nitrosylation]]
-[[Category: Zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 01:00:00 2009''