1p6i: Difference between revisions
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|PDB= 1p6i |SIZE=350|CAPTION= <scene name='initialview01'>1p6i</scene>, resolution 1.90Å | |PDB= 1p6i |SIZE=350|CAPTION= <scene name='initialview01'>1p6i</scene>, resolution 1.90Å | ||
|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=DP3:N-{(4S)-4-AMINO-5-[(2-AMINOETHYL)AMINO]PENTYL}-N'-NITROGUANIDINE'>DP3</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=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= NOS1 OR BNOS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= NOS1 OR BNOS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1p6h|1P6H]], [[1p6j|1P6J]], [[1p6k|1P6K]], [[1p6l|1P6L]], [[1p6m|1P6M]], [[1p6n|1P6N]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6i OCA], [http://www.ebi.ac.uk/pdbsum/1p6i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p6i RCSB]</span> | |||
}} | }} | ||
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[[Category: Silverman, R B.]] | [[Category: Silverman, R B.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
[[Category: heme-enzyme]] | [[Category: heme-enzyme]] | ||
[[Category: nitric oxide synthase]] | [[Category: nitric oxide synthase]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:55:35 2008'' | ||
Revision as of 19:55, 30 March 2008
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| 1p6i, resolution 1.90Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | ACT, DP3, H4B, HEM, ZN | ||||||||||||
| Gene: | NOS1 OR BNOS (Rattus norvegicus) | ||||||||||||
| Activity: | Nitric-oxide synthase, with EC number 1.14.13.39 | ||||||||||||
| Related: | 1P6H, 1P6J, 1P6K, 1P6L, 1P6M, 1P6N
| ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Rat neuronal NOS heme domain with (4S)-N-(4-amino-5-[aminoethyl]aminopentyl)-N'-nitroguanidine bound
Overview
Three nitric oxide synthase (NOS) isoforms, eNOS, nNOS and iNOS, generate nitric oxide (NO) crucial to the cardiovascular, nervous and host defense systems, respectively. Development of isoform-selective NOS inhibitors is of considerable therapeutic importance. Crystal structures of nNOS-selective dipeptide inhibitors in complex with both nNOS and eNOS were solved and the inhibitors were found to adopt a curled conformation in nNOS but an extended conformation in eNOS. We hypothesized that a single-residue difference in the active site, Asp597 (nNOS) versus Asn368 (eNOS), is responsible for the favored binding in nNOS. In the D597N nNOS mutant crystal structure, a bound inhibitor switches to the extended conformation and its inhibition of nNOS decreases >200-fold. Therefore, a single-residue difference is responsible for more than two orders of magnitude selectivity in inhibition of nNOS over eNOS by L-N(omega)-nitroarginine-containing dipeptide inhibitors.
About this Structure
1P6I is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase., Flinspach ML, Li H, Jamal J, Yang W, Huang H, Hah JM, Gomez-Vidal JA, Litzinger EA, Silverman RB, Poulos TL, Nat Struct Mol Biol. 2004 Jan;11(1):54-9. Epub 2003 Dec 29. PMID:14718923
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