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To identify new routes to engineer selectivity, we have discovered a first\u2010in\u2010class p38\u03b4\u2010isoform selective inhibitor reflecting 12\u00a0000\u2010fold selectivity improvement over currently available compounds and superior kinome targeting. X\u2010ray crystallographic characterization indicates that these molecules bind through noncanonical n\u2013\u03c0\u2013\u03c0 stacking sandwich interactions enabled by structural remodeling of the P\u2010loop. Structural and functional analysis indicates that these selective inhibitors are self\u2010encapsulating agents due to direct steric clashing that occludes the binding site in a conformation reinforced by a hydrogen\u2010bonding network involving p38\u03b4\u2010unique H30. This work reveals how inhibitor selectivity is achieved by deliberate remodeling of the drug binding site leveraging structural features outside the binding site commonly overlooked in structure\u2010guided design.<\/jats:p>","DOI":"10.1002\/anie.2953141","type":"journal-article","created":{"date-parts":[[2026,9,16]],"date-time":"2026-09-16T03:24:28Z","timestamp":1789529068000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Thinking Outside the Binding Site: A Self\u2010Encapsulating Kinase Inhibitor Remodels Its Pocket to Achieve Selectivity"],"prefix":"10.1002","author":[{"ORCID":"https:\/\/orcid.org\/0009-0007-4405-2397","authenticated-orcid":false,"given":"Nico J.","family":"Seidler","sequence":"first","affiliation":[{"name":"Department of Chemistry College of Arts and Sciences University at Buffalo The State University of New York  Buffalo New York USA"},{"name":"Institute of Pharmaceutical Sciences 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