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| {{STRUCTURE_2c6z| PDB=2c6z | SCENE= }} | | {{STRUCTURE_2c6z| PDB=2c6z | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I IN COMPLEX WITH CITRULLINE'''
| | ===CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I IN COMPLEX WITH CITRULLINE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16698551}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16698551 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16698551}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: S-nitrosylation]] | | [[Category: S-nitrosylation]] |
| [[Category: Zinc]] | | [[Category: Zinc]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:21:24 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:38:43 2008'' |