2ci7
From Proteopedia
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|PDB= 2ci7 |SIZE=350|CAPTION= <scene name='initialview01'>2ci7</scene>, resolution 1.60Å | |PDB= 2ci7 |SIZE=350|CAPTION= <scene name='initialview01'>2ci7</scene>, resolution 1.60Å | ||
|SITE= <scene name='pdbsite=AC1:GLY+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:GLY+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ci7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ci7 OCA], [http://www.ebi.ac.uk/pdbsum/2ci7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ci7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Grutter, M G.]] | [[Category: Grutter, M G.]] | ||
[[Category: Vasak, M.]] | [[Category: Vasak, M.]] | ||
| - | [[Category: GLY]] | ||
| - | [[Category: ZN]] | ||
[[Category: acetylation]] | [[Category: acetylation]] | ||
[[Category: adma]] | [[Category: adma]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:21:51 2008'' |
Revision as of 23:21, 30 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Dimethylargininase, with EC number 3.5.3.18 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I IN COMPLEX WITH ZINC, HIGH PH
Overview
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.
About this Structure
2CI7 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Mar 31 02:21:51 2008
Categories: Bos taurus | Dimethylargininase | Single protein | Braun, O. | Briand, C. | Frey, D. | Grutter, M G. | Vasak, M. | Acetylation | Adma | Hydrolase | Metal-binding | Mma | No | Nos regulation | S-nitrosylation | Zinc
