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5g0p

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Revision as of 06:49, 26 July 2016

Structure of rat neuronal nitric oxide synthase M336V D597N mutant heme domain in complex with 6-(2-(5-(3-(DIMETHYLAMINO)PROPYL)PYRIDIN- 3-YL)ETHYL)-4-METHYLPYRIDIN-2-AMINE

Structural highlights

5g0p is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	5g0n, 5g0o
Activity:	Nitric-oxide synthase (NADPH dependent), with EC number 1.14.13.39
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NOS1_RAT] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum.

Publication Abstract from PubMed

Development of potent and isoform selective nitric oxide synthase (NOS) inhibitors is challenging because of the structural similarity in the heme active sites. One amino acid difference between NOS isoforms, Asp597 in rat neuronal NOS (nNOS) versus Asn368 in bovine endothelial NOS (eNOS), has been identified as the structural basis for why some dipeptide amide inhibitors bind more tightly to nNOS than to eNOS. We now have found that the same amino acid variation is responsible for substantially different binding modes and affinity for a new class of aminopyridine-based inhibitors.

Electrostatic Control of Isoform Selective Inhibitor Binding in Nitric Oxide Synthase.,Li H, Wang HY, Kang S, Silverman RB, Poulos TL Biochemistry. 2016 Jun 16. PMID:27250740^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li H, Wang HY, Kang S, Silverman RB, Poulos TL. Electrostatic Control of Isoform Selective Inhibitor Binding in Nitric Oxide Synthase. Biochemistry. 2016 Jun 16. PMID:27250740 doi:http://dx.doi.org/10.1021/acs.biochem.6b00261

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5g0p"

Categories: Li, H | Poulos, T L | Inhibitor complex | Nitric oxide synthase | Oxidoreductase

@@ Line 7: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g0n|5g0n]], [[5g0o|5g0o]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5g0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g0p OCA], [http://pdbe.org/5g0p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g0p RCSB], [http://www.ebi.ac.uk/pdbsum/5g0p PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5g0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g0p OCA], [http://pdbe.org/5g0p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g0p RCSB], [http://www.ebi.ac.uk/pdbsum/5g0p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g0p ProSAT]</span></td></tr>
 </table>
 == Function ==

5g0p

From Proteopedia

Revision as of 06:49, 26 July 2016

Structure of rat neuronal nitric oxide synthase M336V D597N mutant heme domain in complex with 6-(2-(5-(3-(DIMETHYLAMINO)PROPYL)PYRIDIN- 3-YL)ETHYL)-4-METHYLPYRIDIN-2-AMINE

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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