{"title":"Room Temperature Serial Synchrotron Crystallography","authors":"K. Hasegawa, T. Kumasaka","doi":"10.5940/jcrsj.64.294","DOIUrl":"https://doi.org/10.5940/jcrsj.64.294","url":null,"abstract":"","PeriodicalId":74311,"journal":{"name":"Nihon Kessho Gakkai shi","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76218755","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Quantum Property and Crystal Structure of Natural Mineral Henmilite","authors":"H. Yamamoto, T. Sakakura, H. Kimura","doi":"10.5940/jcrsj.64.261","DOIUrl":"https://doi.org/10.5940/jcrsj.64.261","url":null,"abstract":"","PeriodicalId":74311,"journal":{"name":"Nihon Kessho Gakkai shi","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85242381","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Structural Insight into an Enzyme that Breaks Down Oligosaccharides in Caramel","authors":"T. Kashima, S. Fushinobu, A. Ishiwata, K. Fujita","doi":"10.5940/jcrsj.64.263","DOIUrl":"https://doi.org/10.5940/jcrsj.64.263","url":null,"abstract":"","PeriodicalId":74311,"journal":{"name":"Nihon Kessho Gakkai shi","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83790292","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Takumi Ueda, Yutaka Kofuku, K. Takeuchi, Shunsuke Imai, Yutaro Shiraishi, I. Shimada
NMR methods provide information about conformational dynamics of GPCRs over a wide range of frequencies in aqueous media at near-physiological temperature, with minimal modification of the wild-type GPCR covalent structures. Here we review our solution NMR studies of the function-related conformational dynamics of GPCRs, including β 2 adrenergic receptor, μ opioid receptor
{"title":"Function-Related Conformational Dynamics of GPCRs Revealed by Solution NMR","authors":"Takumi Ueda, Yutaka Kofuku, K. Takeuchi, Shunsuke Imai, Yutaro Shiraishi, I. Shimada","doi":"10.5940/jcrsj.64.279","DOIUrl":"https://doi.org/10.5940/jcrsj.64.279","url":null,"abstract":"NMR methods provide information about conformational dynamics of GPCRs over a wide range of frequencies in aqueous media at near-physiological temperature, with minimal modification of the wild-type GPCR covalent structures. Here we review our solution NMR studies of the function-related conformational dynamics of GPCRs, including β 2 adrenergic receptor, μ opioid receptor","PeriodicalId":74311,"journal":{"name":"Nihon Kessho Gakkai shi","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90417721","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Protein-protein interactions are essential in diverse cellular processes including signal transduction. It is not uncommon for protein-protein interactions in the transmembrane signaling to exhibit low binding affinities with a dissociation constant in the μM range or higher. Presumably, membrane proteins can selectively bind with their binding partners via low-affinity interactions because they can only diffuse laterally in the membrane plane and interact with the partners within a limited space on the membrane surface or within the membrane. This review focuses on the crystallographic studies on cell-surface receptors and intramembrane proteases that perform the transmembrane signaling mediated by low-affinity protein-protein interactions.
{"title":"Structural Biology on Molecular Mechanism of Low-Affinity Protein-Protein Interactions on the Cell Membrane","authors":"T. Nogi","doi":"10.5940/jcrsj.64.269","DOIUrl":"https://doi.org/10.5940/jcrsj.64.269","url":null,"abstract":"Protein-protein interactions are essential in diverse cellular processes including signal transduction. It is not uncommon for protein-protein interactions in the transmembrane signaling to exhibit low binding affinities with a dissociation constant in the μM range or higher. Presumably, membrane proteins can selectively bind with their binding partners via low-affinity interactions because they can only diffuse laterally in the membrane plane and interact with the partners within a limited space on the membrane surface or within the membrane. This review focuses on the crystallographic studies on cell-surface receptors and intramembrane proteases that perform the transmembrane signaling mediated by low-affinity protein-protein interactions.","PeriodicalId":74311,"journal":{"name":"Nihon Kessho Gakkai shi","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88804673","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"X-ray Crystallographic Analysis of Copper Amine Oxidase in Physiological Environments using Humid Air and Glue-coating(HAG)Method","authors":"S. Baba, T. Murakawa","doi":"10.5940/jcrsj.64.285","DOIUrl":"https://doi.org/10.5940/jcrsj.64.285","url":null,"abstract":"","PeriodicalId":74311,"journal":{"name":"Nihon Kessho Gakkai shi","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84684701","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}