{"created":"2024-12-12T02:02:38.380303+00:00","id":2009706,"links":{},"metadata":{"_buckets":{"deposit":"c99d5a6c-1c07-4174-89ce-06cc726a9816"},"_deposit":{"created_by":7,"id":"2009706","owners":[7],"pid":{"revision_id":0,"type":"depid","value":"2009706"},"status":"published"},"_oai":{"id":"oai:tokushima-u.repo.nii.ac.jp:02009706","sets":["1713853213384:1713853295607"]},"author_link":["1117","751","865","1586","1582","1162","1294","282","866"],"control_number":"2009706","item_10001_alternative_title_1":{"attribute_name":"タイトル別表記","attribute_value_mlt":[{"subitem_alternative_title":"Structure of MSPL–inhibitor complex","subitem_alternative_title_language":"en"}]},"item_10001_biblio_info_7":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2021-04-05","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"6","bibliographicPageStart":"e202000849","bibliographicVolumeNumber":"4","bibliographic_titles":[{"bibliographic_title":"Life Science Alliance","bibliographic_titleLang":"en"}]}]},"item_10001_description_5":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"Infection of certain influenza viruses is triggered when its HA is cleaved by host cell proteases such as proprotein convertases and type II transmembrane serine proteases (TTSP). HA with a monobasic motif is cleaved by trypsin-like proteases, including TMPRSS2 and HAT, whereas the multibasic motif found in high pathogenicity avian influenza HA is cleaved by furin, PC5/6, or MSPL. MSPL belongs to the TMPRSS family and preferentially cleaves [R/K]-K-K-R↓ sequences. Here, we solved the crystal structure of the extracellular region of human MSPL in complex with an irreversible substrate-analog inhibitor. The structure revealed three domains clustered around the C-terminal α-helix of the SPD. The inhibitor structure and its putative model show that the P1-Arg inserts into the S1 pocket, whereas the P2-Lys and P4-Arg interacts with the Asp/Glu-rich 99-loop that is unique to MSPL. Based on the structure of MSPL, we also constructed a homology model of TMPRSS2, which is essential for the activation of the SARS-CoV-2 spike protein and infection. The model may provide the structural insight for the drug development for COVID-19.","subitem_description_language":"en","subitem_description_type":"Abstract"}]},"item_10001_publisher_8":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Life Science Alliance","subitem_publisher_language":"en"}]},"item_10001_rights_15":{"attribute_name":"権利情報","attribute_value_mlt":[{"subitem_rights":"This article is available under a Creative Commons License (Attribution 4.0 International, as described at 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