1d1v: Difference between revisions
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|PDB= 1d1v |SIZE=350|CAPTION= <scene name='initialview01'>1d1v</scene>, resolution 1.93Å | |PDB= 1d1v |SIZE=350|CAPTION= <scene name='initialview01'>1d1v</scene>, resolution 1.93Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CAD:CACODYLIC+ACID'>CAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PTU:2-ETHYL-1-PHENYL-ISOTHIOUREA'>PTU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | ||
|ACTIVITY= [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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1nse|1NSE]], [[1d0c|1D0C]], [[1d0o|1D0O]], [[1d0p|1D0P]], [[1d1v|1D1V]], [[1d1w|1D1W]], [[1d1x|1D1X]], [[1d1y|1D1Y]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1v OCA], [http://www.ebi.ac.uk/pdbsum/1d1v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d1v RCSB]</span> | |||
}} | }} | ||
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[[Category: Raman, C S.]] | [[Category: Raman, C S.]] | ||
[[Category: Southan, G J.]] | [[Category: Southan, G J.]] | ||
[[Category: alpha-beta fold]] | [[Category: alpha-beta fold]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:32:54 2008'' | ||
Revision as of 19:32, 30 March 2008
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| , resolution 1.93Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||
| Related: | 1NSE, 1D0C, 1D0O, 1D0P, 1D1V, 1D1W, 1D1X, 1D1Y
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE ENDOTHELIAL NITRIC OXIDE SYNTHASE HEME DOMAIN COMPLEXED WITH S-ETHYL-N-PHENYL-ISOTHIOUREA (H4B BOUND)
OverviewOverview
Nitric oxide produced by nitric-oxide synthase (NOS) is not only involved in a wide range of physiological functions but also in a variety of pathological conditions. Isoform-selective NOS inhibitors are highly desirable to regulate the NO production of one isoform beneficial to normal physiological functions from the uncontrolled NO production of another isoform that accompanies certain pathological states. Crystal structures of the heme domain of the three NOS isoforms have revealed a very high degree of similarity in the immediate vicinity of the heme active site illustrating the challenge of isoform-selective inhibitor design. Isothioureas are potent NOS inhibitors, and the structures of the endothelial NOS heme domain complexed with isothioureas bearing small S-alkyl substituents have been determined (Li, H., Raman, C.S., Martasek, P., Kral, V., Masters, B.S.S., and Poulos, T.L. (2000) J. Inorg. Biochem. 81, 133--139). In the present communication, the binding mode of larger bisisothioureas complexed to the endothelial NOS heme domain has been determined. These structures afford a structural rationale for the known inhibitory activities. In addition, these structures provide clues on how to exploit the longer inhibitor substituents that extend out of the active site pocket for isoform-selective inhibitor design.
About this StructureAbout this Structure
1D1V is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase., Raman CS, Li H, Martasek P, Babu BR, Griffith OW, Masters BS, Poulos TL, J Biol Chem. 2001 Jul 13;276(28):26486-91. Epub 2001 Apr 30. PMID:11331290
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