2ci6: Difference between revisions
New page: left|200px<br /> <applet load="2ci6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ci6, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O... |
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==About this Structure== | ==About this Structure== | ||
2CI6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.18 3.5.3.18]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CI6 OCA]]. | 2CI6 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CI6 OCA]]. | ||
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16698551 16698551] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16698551 16698551] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Dimethylargininase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Braun, O.]] | [[Category: Braun, O.]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
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Revision as of 15:06, 30 October 2007
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CRYSTAL STRUCTURE OF DIMETHYLARGININE DIMETHYLAMINOHYDROLASE I BOUND WITH ZINC LOW PH
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
2CI6 is a [Single protein] structure of sequence from [Bos taurus] with ZN as [ligand]. Active as [Dimethylargininase], with EC number [3.5.3.18]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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
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