4nos

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(New page: 200px<br /> <applet load="4nos" size="450" color="white" frame="true" align="right" spinBox="true" caption="4nos, resolution 2.250&Aring;" /> '''HUMAN INDUCIBLE NI...)
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<applet load="4nos" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="4nos, resolution 2.250&Aring;" />
caption="4nos, resolution 2.250&Aring;" />
'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR'''<br />
'''HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR'''<br />
==Overview==
==Overview==
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Crystal structures of human endothelial nitric oxide synthase (eNOS) and, human inducible NOS (iNOS) catalytic domains were solved in complex with, the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger, active-site cavity containing heme and tetrahydrobiopterin. Both are, hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The, active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective, inhibitors. The high-resolution, refined structures of eNOS (2.4 A, resolution) and iNOS (2.25 A resolution) reveal an unexpected structural, zinc situated at the intermolecular interface and coordinated by four, cysteines, two from each monomer.
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Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 A resolution) and iNOS (2.25 A resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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4NOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN, HEM, H2B, ITU and H4B 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=4NOS OCA].
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4NOS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=H2B:'>H2B</scene>, <scene name='pdbligand=ITU:'>ITU</scene> and <scene name='pdbligand=H4B:'>H4B</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=4NOS OCA].
==Reference==
==Reference==
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[[Category: Nitric-oxide synthase]]
[[Category: Nitric-oxide synthase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Fischmann, T.O.]]
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[[Category: Fischmann, T O.]]
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[[Category: Weber, P.C.]]
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[[Category: Weber, P C.]]
[[Category: H2B]]
[[Category: H2B]]
[[Category: H4B]]
[[Category: H4B]]
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[[Category: zns4]]
[[Category: zns4]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:51:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:52 2008''

Revision as of 17:13, 21 February 2008


4nos, resolution 2.250Å

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HUMAN INDUCIBLE NITRIC OXIDE SYNTHASE WITH INHIBITOR

Contents

Overview

Crystal structures of human endothelial nitric oxide synthase (eNOS) and human inducible NOS (iNOS) catalytic domains were solved in complex with the arginine substrate and an inhibitor S-ethylisothiourea (SEITU), respectively. The small molecules bind in a narrow cleft within the larger active-site cavity containing heme and tetrahydrobiopterin. Both are hydrogen-bonded to a conserved glutamate (eNOS E361, iNOS E377). The active-site residues of iNOS and eNOS are nearly identical. Nevertheless, structural comparisons provide a basis for design of isozyme-selective inhibitors. The high-resolution, refined structures of eNOS (2.4 A resolution) and iNOS (2.25 A resolution) reveal an unexpected structural zinc situated at the intermolecular interface and coordinated by four cysteines, two from each monomer.

Disease

Known diseases associated with this structure: Hypertension, susceptibility to OMIM:[163730], Malaria, resistance to OMIM:[163730]

About this Structure

4NOS is a Single protein structure of sequence from Homo sapiens with , , , and as ligands. Active as Nitric-oxide synthase, with EC number 1.14.13.39 Full crystallographic information is available from OCA.

Reference

Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation., Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC, Nat Struct Biol. 1999 Mar;6(3):233-42. PMID:10074942

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