{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1390282679364756992.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1246/nikkashi.1987.580"}},{"identifier":{"@type":"NDL_BIB_ID","@value":"3118492"}},{"identifier":{"@type":"URI","@value":"http://id.ndl.go.jp/bib/3118492"}},{"identifier":{"@type":"URI","@value":"https://ndlsearch.ndl.go.jp/books/R000000004-I3118492"}},{"identifier":{"@type":"URI","@value":"https://www.jstage.jst.go.jp/article/nikkashi1972/1987/3/1987_3_580/_pdf"}},{"identifier":{"@type":"NAID","@value":"130004158662"}},{"identifier":{"@type":"NAID","@value":"40002844677"}},{"identifier":{"@type":"URI","@value":"https://search.jamas.or.jp/link/ui/1987182465"}}],"dc:title":[{"@language":"en","@value":"Transmittance by Acetylcholine at Nicotinic Synapses Structure and Function of Nicotinic Acetylcholine Receptor"},{"@language":"ja","@value":"シナプスにおけるアセチルコリンの受容ニコチン性アセチルコリン受容体の分子構造と機能"},{"@language":"ja-Kana","@value":"シナプス ニ オケル アセチルコリン ノ ジュヨウ ニコチンセイ アセチルコリ"}],"description":[{"type":"abstract","notation":[{"@language":"en","@value":"Nicotinic acetylcholine receptor (nAChR) is a membrane glycoprotein which functions as a transmitter receptor at vertebrate neuromuscular synapses. nAChR from the electric organ of electric fishes consists of four kinds of subunits assembled in a molar stoichiometry of α<SUB>2</SUB>βγδ. The primary, structures of all these four subunits and those from some mammalian muscle nAChR have been elucidated by cloning and sequencing cDNAs, or genomic DNA endoding these polypeptides. The four subunits have marked sequence homology and are similar in hydrophilicity profile and predicted secondary structure, thus oriented most probably in a pseudosymmetric fashion across the membrane. Eachsubunit is supposed to have five transmembrane domains, one of which is amphipathic and has both charged and uncharged polar residues on one side of an α-helix and nonpolar residues on the opposite side. Thus these amphipathic segments of all subunits may form the ion, channel. The α subunit has been shown by affinity labelling to bear a functional acety lcholine binding site. This site also binds antagonists, such as (+)-tubocurarine or neurotoxins from snake venoms. nAChR contains two binding sites per receptor monomer. The reactivi-ties of the two binding sites are not identical. These differences have been considereddue to the structural, asymmetry of the receptor. Recently Cys-192 and Cys-193 of the α subunit were postulated to concern in the acetylcholine binding site And are disulfide-crosslinked each other. It is suggested that a transition between two stble conformations of the vicinal disulfide is associated with receptor activation by agonists. More recently, we elucidated the carbohydrate structures of the receptor. More than 70% of the total oligosaccharide chains in Torpedo nAChR ate of the high-mannose type with the structures Man<SUB>8</SUB>GlcNAc<SUB>2</SUB> and Man<SUB>9</SUB>GlcNAc<SUB>2</SUB>. These two types of oligosaccharides are shown to be distributed in different proportions in all the subunits. It was also found that several kinds of complex-type oligosaccharides comprising the rest of the carbohydrate moiety in the protein exist mainly in the γ and δ subunits. Although the chemical structures of nAChRs are well characterized, the relationship between structure and function remains to be clarified. The elucidation qf he three-dimensional structure of nAChR by X-ray analysis will open the way to a better understanding of the problem."},{"@language":"ja","@value":"ニコチン性アセチルコリン受容体(nAChR)は,脊椎動物の神経筋接合部や電気魚電気器官に存在し,神経終末から放出されるアセチルコリンに応答して,陽イオンの透過性を増大させる機能をもつ膜糖タンパク質である。nAChRは,α2βγδという4種のサブユニットからなる五量体構造をもち, nAChR,としてのすべての機能はこの分子中に含まれている.最近,電気魚やいくつかの哺乳動物のnACbRサブユニットの一次構造が,遣伝子組み換え技術を用いて解明されたが,四つのサブユニットは相互に高い類似性を有しており,擬対称的に配列しているものと考えられる。これらのサブユニットは,それぞれ五つの膜貫通ドメインをもち,そのうちの一つは両親媒性のドメインで,イオンチャンネルの形成に寄与していると推測される。サブユニットのうち,δサブユニットはイオンチャンネルの開口時間を決定する機能をもつ。また,ウシのnAChRでは,発生過程で構成サブユニットが変化する可能性が示唆されている。<BR>αサブユニットはAChと結合する機能をもち,したがってnAChR単量体あたり二つの結合部位が存在することになるが,これらの反応性は等しくない。この違いは,受容体の構造的非対称性によるもらのと思われる。最近,αサブユニットのCys192とCys193の間でS-S橋が形成され,しかもこれらの残基がアセチルコリン結合部位の近傍に位置することが解明された。アゴニストの結合により,この隣合うCys残基間のS-S橋は配座変化を起こし,イオンチャネルの開口へ受容体を誘導すると考えられる。<BR>著者らに最近T.californica AChRの糖鎖構造を明らかにしたが,2種のハイマンノース型糖鎖,Man<SUB>8</SUB>GlcNAc<SUB>2</SUB>とMan<SUB>9</SUB>GlcNAc<SUB>2</SUB>が全体の70%以上を占めており,これらの糖鎖はすべてのサブユニットに,異なった割合で存在していた。その他の糖鎖は数種類のコンプレックス型糖鎖で,おもにγとδサブユニットに存在した。これらの糖鎖のリガンドとの結合における関与を検討したところ,シアル酸やハイマンノース型糖鎖を除いてもほとんど影響を受けないことがわかった。nAChRの化学構造はかなり解明されつつあるが, 構造と機能の関連に関しては不明な点が多い。また,nAChRのリン酸化や受容体に密接して存在する43Kタンパク質などの機能がさらに明らかになれば,nAChRの働きに関する理解が一層進むものと思われる。"}],"abstractLicenseFlag":"disallow"}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1030003658366100224","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"80164747"},{"@type":"NRID","@value":"1000080164747"},{"@type":"NRID","@value":"9000002271922"},{"@type":"NRID","@value":"9000403938414"},{"@type":"NRID","@value":"9000400186268"},{"@type":"NRID","@value":"9000391553568"},{"@type":"NRID","@value":"9000391554595"},{"@type":"NRID","@value":"9000391575158"},{"@type":"NRID","@value":"9000283437400"},{"@type":"NRID","@value":"9000283445610"},{"@type":"NRID","@value":"9000257923005"},{"@type":"NRID","@value":"9000391578727"},{"@type":"NRID","@value":"9000403938442"},{"@type":"NRID","@value":"9000403936472"},{"@type":"NRID","@value":"9000007036705"},{"@type":"NRID","@value":"9000391574600"},{"@type":"NRID","@value":"9000256046396"},{"@type":"NRID","@value":"9000257923180"},{"@type":"NRID","@value":"9000002277660"},{"@type":"NRID","@value":"9000400185756"},{"@type":"NRID","@value":"9000256738728"},{"@type":"NRID","@value":"9000283442894"},{"@type":"NRID","@value":"9000014533742"},{"@type":"NRID","@value":"9000400186280"},{"@type":"NRID","@value":"9000402084510"},{"@type":"NRID","@value":"9000283437433"},{"@type":"NRID","@value":"9000002270986"},{"@type":"NRID","@value":"9000021906410"},{"@type":"NRID","@value":"9000021572850"},{"@type":"NRID","@value":"9000402084500"},{"@type":"NRID","@value":"9000021563277"},{"@type":"NRID","@value":"9000021394136"},{"@type":"NRID","@value":"9000391564454"},{"@type":"NRID","@value":"9000283441493"},{"@type":"NRID","@value":"9000391584408"},{"@type":"NRID","@value":"9000391570748"},{"@type":"NRID","@value":"9000391570403"},{"@type":"NRID","@value":"9000391574313"},{"@type":"NRID","@value":"9000400184981"},{"@type":"NRID","@value":"9000391554093"},{"@type":"NRID","@value":"9000391567609"},{"@type":"NRID","@value":"9000253568205"},{"@type":"NRID","@value":"9000283442563"},{"@type":"NRID","@value":"9000403936470"},{"@type":"NRID","@value":"9000391570653"},{"@type":"NRID","@value":"9000283443894"},{"@type":"NRID","@value":"9000021118915"},{"@type":"NRID","@value":"9000391561818"},{"@type":"NRID","@value":"9000391572526"},{"@type":"NRID","@value":"9000256742005"},{"@type":"NRID","@value":"9000403938427"},{"@type":"NRID","@value":"9000391575206"},{"@type":"NRID","@value":"9000400184990"},{"@type":"NRID","@value":"9000257923278"},{"@type":"NRID","@value":"9000002278413"},{"@type":"NRID","@value":"9000400184997"},{"@type":"NRID","@value":"9000021412232"},{"@type":"NRID","@value":"9000021457245"},{"@type":"NRID","@value":"9000022156719"},{"@type":"NRID","@value":"9000391579604"},{"@type":"NRID","@value":"9000402085348"},{"@type":"NRID","@value":"9000391582422"},{"@type":"NRID","@value":"9000283440758"},{"@type":"NRID","@value":"9000283496998"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/read0020137"}],"foaf:name":[{"@language":"en","@value":"NOMOTO 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Kyozo"},{"@language":"ja","@value":"林 恭三"}],"jpcoar:affiliationName":[{"@language":"ja","@value":"岐阜薬科大学"},{"@language":"en","@value":"Gifu Pharmaceutical University"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"03694577"},{"@type":"EISSN","@value":"21850925"},{"@type":"NDL_BIB_ID","@value":"000000018251"},{"@type":"ISSN","@value":"03694577"},{"@type":"LISSN","@value":"03694577"},{"@type":"NCID","@value":"AN00186595"}],"prism:publicationName":[{"@language":"en","@value":"NIPPON KAGAKU KAISHI"},{"@language":"ja","@value":"日本化学会誌（化学と工業化学）"},{"@language":"en","@value":"Nippon Kagaku Kaishi"},{"@language":"ja","@value":"日化"},{"@language":"en","@value":"NIPPON KAGAKU KAISHI"},{"@language":"ja","@value":"日本化学会誌"}],"dc:publisher":[{"@language":"en","@value":"The Chemical Society of Japan"},{"@language":"ja","@value":"公益社団法人 日本化学会"}],"prism:publicationDate":"1987-03-10","prism:volume":"1987","prism:number":"3","prism:startingPage":"580","prism:endingPage":"588"},"reviewed":"false","url":[{"@id":"http://id.ndl.go.jp/bib/3118492"},{"@id":"https://ndlsearch.ndl.go.jp/books/R000000004-I3118492"},{"@id":"https://www.jstage.jst.go.jp/article/nikkashi1972/1987/3/1987_3_580/_pdf"},{"@id":"https://search.jamas.or.jp/link/ui/1987182465"}],"availableAt":"1987-03-10","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=General%20Chemistry","dc:title":"General Chemistry"}],"dataSourceIdentifier":[{"@type":"JALC","@value":"oai:japanlinkcenter.org:0017179030"},{"@type":"NDL_SEARCH","@value":"oai:ndlsearch.ndl.go.jp:R000000004-I3118492"},{"@type":"CROSSREF","@value":"10.1246/nikkashi.1987.580"},{"@type":"CIA","@value":"130004158662"},{"@type":"CIA","@value":"40002844677"}]}