1ed4

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(New page: 200px<br /><applet load="1ed4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ed4, resolution 1.86&Aring;" /> '''BOVINE ENDOTHELIAL N...)
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[[Image:1ed4.gif|left|200px]]<br /><applet load="1ed4" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ed4.gif|left|200px]]<br /><applet load="1ed4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ed4, resolution 1.86&Aring;" />
caption="1ed4, resolution 1.86&Aring;" />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)'''<br />
'''BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)'''<br />
==Overview==
==Overview==
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Analyzing the active site topology and plasticity of nitric oxide synthase, (NOS) and understanding enzyme-drug interactions are crucial for the, development of potent, isoform-selective NOS inhibitors. A small, hydrophobic pocket in the active site is identified in the bovine eNOS, heme domain structures complexed with potent isothiourea inhibitors:, seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and, 2-aminothiazoline, respectively. These structures reveal the importance of, nonpolar van der Waals contacts in addition to the well-known hydrogen, bonding interactions between inhibitor and enzyme. The scaffold of a, potent NOS inhibitor should be capable of donating hydrogen bonds to as, well as making nonpolar contacts with amino acids in the NOS active site.
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Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.
==About this Structure==
==About this Structure==
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1ED4 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 ACT, ZN, HEM, IPU, CAD and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ED4 OCA].
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1ED4 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 <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=IPU:'>IPU</scene>, <scene name='pdbligand=CAD:'>CAD</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitric-oxide_synthase Nitric-oxide synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ED4 OCA].
==Reference==
==Reference==
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[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: Martasek, P.]]
[[Category: Martasek, P.]]
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[[Category: Masters, B.S.S.]]
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[[Category: Masters, B S.S.]]
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[[Category: Poulos, T.L.]]
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[[Category: Poulos, T L.]]
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[[Category: Raman, C.S.]]
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[[Category: Raman, C S.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: CAD]]
[[Category: CAD]]
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[[Category: nitric oxide synthase]]
[[Category: nitric oxide synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:54:31 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:30 2008''

Revision as of 10:26, 21 February 2008

Image:1ed4.gif

1ed4, resolution 1.86Å

Drag the structure with the mouse to rotate

BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH IPITU (H4B FREE)

Overview

Analyzing the active site topology and plasticity of nitric oxide synthase (NOS) and understanding enzyme-drug interactions are crucial for the development of potent, isoform-selective NOS inhibitors. A small hydrophobic pocket in the active site is identified in the bovine eNOS heme domain structures complexed with potent isothiourea inhibitors: seleno analogue of S-ethyl-isothiourea, S-isopropyl-isothiourea, and 2-aminothiazoline, respectively. These structures reveal the importance of nonpolar van der Waals contacts in addition to the well-known hydrogen bonding interactions between inhibitor and enzyme. The scaffold of a potent NOS inhibitor should be capable of donating hydrogen bonds to as well as making nonpolar contacts with amino acids in the NOS active site.

About this Structure

1ED4 is a Single protein structure of sequence from Bos taurus with , , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

Reference

Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas., Li H, Raman CS, Martasek P, Kral V, Masters BS, Poulos TL, J Inorg Biochem. 2000 Aug 31;81(3):133-9. PMID:11051558

Page seeded by OCA on Thu Feb 21 12:26:30 2008

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