2ci5

<table><tr><td colspan='2'>[[2ci5]] is a 2 chain structure with 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=2CI5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CI5 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c6z|2c6z]], [[2ci1|2ci1]], [[2ci3|2ci3]], [[2ci4|2ci4]], [[2ci6|2ci6]], [[2ci7|2ci7]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dimethylargininase Dimethylargininase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.18 3.5.3.18] </span></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=2ci5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ci5 OCA], [http://pdbe.org/2ci5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ci5 RCSB], [http://www.ebi.ac.uk/pdbsum/2ci5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ci5 ProSAT]</span></td></tr>

[[http://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.

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== 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.

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>

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<div class="pdbe-citations 2ci5" style="background-color:#fffaf0;"></div>

==See Also==

*[[Dimethylarginine Dimethylaminohydrolase|Dimethylarginine Dimethylaminohydrolase]]

== References ==

<references/>

[[Category: Dimethylargininase]]

[[Category: Braun, O]]

[[Category: Briand, C]]

[[Category: Frey, D]]

[[Category: Grutter, M G]]

[[Category: Vasak, M]]

[[Category: Zinc]]