1qau

<table><tr><td colspan='2'>[[1qau]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QAU FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qau OCA], [https://pdbe.org/1qau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qau RCSB], [https://www.ebi.ac.uk/pdbsum/1qau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qau ProSAT]</span></td></tr>

[[https://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.

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== Publication Abstract from PubMed ==

The PDZ protein interaction domain of neuronal nitric oxide synthase (nNOS) can heterodimerize with the PDZ domains of postsynaptic density protein 95 and syntrophin through interactions that are not mediated by recognition of a typical carboxyl-terminal motif. The nNOS-syntrophin PDZ complex structure revealed that the domains interact in an unusual linear head-to-tail arrangement. The nNOS PDZ domain has two opposite interaction surfaces-one face has the canonical peptide binding groove, whereas the other has a beta-hairpin "finger." This nNOS beta finger docks in the syntrophin peptide binding groove, mimicking a peptide ligand, except that a sharp beta turn replaces the normally required carboxyl terminus. This structure explains how PDZ domains can participate in diverse interaction modes to assemble protein networks.

Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex.,Hillier BJ, Christopherson KS, Prehoda KE, Bredt DS, Lim WA Science. 1999 Apr 30;284(5415):812-5. PMID:10221915<ref>PMID:10221915</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Bredt, D S]]

[[Category: Christopherson, K S]]

[[Category: Hillier, B J]]

[[Category: Lim, W A]]

[[Category: Prehoda, K E]]

[[Category: Beta-finger]]

[[Category: Oxidoreductase]]