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Specific inhibition of\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 activity may be a promising target for therapy for diseases characterized by dysregulated\n                    <jats:styled-content style=\"fixed-case\">ECM<\/jats:styled-content>\n                    turnover. Potent\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 inhibitors including an indole scaffold were recently reported in an\n                    <jats:styled-content style=\"fixed-case\">X<\/jats:styled-content>\n                    \u2010ray crystallographic study. Herein, we addressed whether melatonin, a secretory product of pineal gland, has an inhibitory effect on\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 function. Gelatin zymographic analysis showed a significant reduction in pro\u2010 and active\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 activity in vitro in a dose\u2010 and time\u2010dependent manner. In addition, a human gastric adenocarcinoma cell line (\n                    <jats:styled-content style=\"fixed-case\">AGS<\/jats:styled-content>\n                    ) exhibited a reduced (~50%)\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 expression when incubated with melatonin, supporting an inhibitory effect of melatonin on\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109. Atomic\u2010level interaction between melatonin and\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 was probed with computational chemistry tools. Melatonin docked into the active site cleft of\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109 and interacted with key catalytic site residues including the three histidines that form the coordination complex with the catalytic zinc as well as proline 421 and alanine 191. We hypothesize that under physiological conditions, tight binding of melatonin in the active site might be involved in reducing the catalytic activity of\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109. This finding could provide a novel approach to physical docking of biomolecules to the catalytic site of\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    s, which inhibits this protease, to arrest\n                    <jats:styled-content style=\"fixed-case\">MMP<\/jats:styled-content>\n                    \u20109\u2010mediated inflammatory signals.\n                  <\/jats:p>","DOI":"10.1111\/jpi.12034","type":"journal-article","created":{"date-parts":[[2012,12,27]],"date-time":"2012-12-27T10:10:22Z","timestamp":1356603022000},"page":"398-405","source":"Crossref","is-referenced-by-count":113,"title":["Melatonin inhibits matrix metalloproteinase\u20109 activity by binding to its active site"],"prefix":"10.1111","volume":"54","author":[{"given":"Deep Sankar","family":"Rudra","sequence":"first","affiliation":[{"name":"Drug Development Diagnostics and Biotechnology Division Department of Physiology Indian Institute of 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