{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T09:47:41Z","timestamp":1791107261756,"version":"4.1.0"},"reference-count":30,"publisher":"Wiley","issue":"28","license":[{"start":{"date-parts":[[2008,10,31]],"date-time":"2008-10-31T00:00:00Z","timestamp":1225411200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2008,11,26]]},"abstract":"<jats:p>\n                    Creatine kinase is a member of the phosphagen kinase family, which catalyzes the reversible phosphoryl transfer reaction that occurs between ATP and creatine to produce ADP and phosphocreatine. Here, three structural aspects of human\u2010brain\u2010type\u2010creatine\u2010kinase (\n                    <jats:italic>h<\/jats:italic>\n                    BB\u2010CK) were identified by X\u2010ray crystallography: the ligand\u2010free\u2010form at 2.2 \u00c5; the ADP\u2013Mg\n                    <jats:sup>2+<\/jats:sup>\n                    , nitrate, and creatine complex (transition\u2010state\u2010analogue complex; TSAC); and the ADP\u2013Mg\n                    <jats:sup>2+<\/jats:sup>\n                    \u2010complex at 2.0 \u00c5. The structures of ligand\u2010bound\n                    <jats:italic>h<\/jats:italic>\n                    BB\u2010CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP\u2013Mg\n                    <jats:sup>2+<\/jats:sup>\n                    \u2010complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP\u2013Mg\n                    <jats:sup>2+<\/jats:sup>\n                    alone may trigger conformational changes in\n                    <jats:italic>h<\/jats:italic>\n                    BB\u2010CK that were not observed with muscle\u2010type\u2010CK.\n                  <\/jats:p>","DOI":"10.1016\/j.febslet.2008.10.039","type":"journal-article","created":{"date-parts":[[2008,11,1]],"date-time":"2008-11-01T04:22:26Z","timestamp":1225513346000},"page":"3959-3965","source":"Crossref","is-referenced-by-count":76,"title":["Structural studies of human brain\u2010type creatine kinase complexed with the ADP\u2013Mg\n                    <sup>2+<\/sup>\n                    \u2013NO\n                    <sup>3\u2212<\/sup>\n                    \u2013creatine transition\u2010state analogue complex"],"prefix":"10.1002","volume":"582","author":[{"given":"Seoung Min","family":"Bong","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jin Ho","family":"Moon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ki Hyun","family":"Nam","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ki Seog","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Young Min","family":"Chi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kwang Yeon","family":"Hwang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2008,10,31]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1006\/exnr.1997.6550"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M201777200"},{"key":"e_1_2_5_4_1","first-page":"295","article-title":"Overexpression, purification and preliminary X-ray crystallographic analysis of human brain-type creatine kinase","volume":"18","author":"Bong S.M.","year":"2008","journal-title":"J. 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