1b8q

From Proteopedia

(Difference between revisions)

Revision as of 23:18, 24 December 2014

SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE

Structural highlights

1b8q is a 2 chain structure with sequence from Rattus norvegicus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The PDZ domain of neuronal nitric oxide synthase (nNOS) functions as a scaffold for organizing the signal transduction complex of the enzyme. The NMR structure of a complex composed of the nNOS PDZ domain and an associated peptide suggests that a two-stranded beta-sheet C-terminal to the canonical PDZ domain may mediate its interaction with the PDZ domains of postsynaptic density-95 and alpha-syntrophin. The structure also provides the molecular basis of recognition of Asp-X-Val-COOH peptides by the nNOS PDZ domain. The role of the C-terminal extension in Asp-X-Val-COOH peptide binding is investigated. Additionally, NMR studies further show that the Asp-X-Val-COOH peptide and a C-terminal peptide from a novel cytosolic protein named CAPON bind to the same pocket of the nNOS PDZ domain.

Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide.,Tochio H, Zhang Q, Mandal P, Li M, Zhang M Nat Struct Biol. 1999 May;6(5):417-21. PMID:10331866^[1]

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

References

↑ Tochio H, Zhang Q, Mandal P, Li M, Zhang M. Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide. Nat Struct Biol. 1999 May;6(5):417-21. PMID:10331866 doi:10.1038/8216

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1b8q"

@@ Line 5: / Line 5: @@
 </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=1b8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b8q RCSB], [http://www.ebi.ac.uk/pdbsum/1b8q PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/NOS1_RAT 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1b8q

From Proteopedia

Revision as of 23:18, 24 December 2014

SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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