{"id":{"repo_id":"gmu","oai_identifier":"oai:MARS:1920/11650"},"canonical_url":"https://search.dev.ndltd.org/etd/gmu/oai:MARS:1920/11650","repository":{"repo_id":"gmu","name":"George Mason University","base_url":"https://mars.gmu.edu/server/oai/request"},"display":{"title":"Molecular Dynamics Simulations on the Interleukin-1β:Interleukin Receptor I:Interleukin-1 Receptor Accessory Protein Ternary Complex","abstract":"Osteoarthritis affects millions of people worldwide each year. The inflammatory signaling pathway associated with osteoarthritis contains a possible novel drug target, the IL-1β ternary complex. IL-1β interacts with two associated proteins, IL-1RI and IL-1RAcP, to exert downstream inflammatory effects. Experimental studies of this complex have identified residue Arg-286 of IL-1RAcP as a “hot spot” of interaction. This paper aimed to computationally study the IL-1β complex with molecular mechanical and quantum mechanical methods. The study found Arg-286 of IL-1RAcP to be the hot spot, participating in a hydrogen bond with Asp-54 of IL- 1β. In agreement with previous experimental studies, Arg-286 was identified as a possible target for drug discovery aimed at inhibiting IL-1β complex and its ultimate downstream inflammatory effects.","abstract_html":"Osteoarthritis affects millions of people worldwide each year. The inflammatory signaling pathway associated with osteoarthritis contains a possible novel drug target, the IL-1β ternary complex. IL-1β interacts with two associated proteins, IL-1RI and IL-1RAcP, to exert downstream inflammatory effects. Experimental studies of this complex have identified residue Arg-286 of IL-1RAcP as a “hot spot” of interaction. This paper aimed to computationally study the IL-1β complex with molecular mechanical and quantum mechanical methods. The study found Arg-286 of IL-1RAcP to be the hot spot, participating in a hydrogen bond with Asp-54 of IL- 1β. In agreement with previous experimental studies, Arg-286 was identified as a possible target for drug discovery aimed at inhibiting IL-1β complex and its ultimate downstream inflammatory effects.","abstract_has_math":false,"creators":["Joshi, Reva"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":null,"date_issued":"","date_published":null,"updated_at":"2026-07-27T19:51:52Z","subjects":["Molecular dynamics","Fragment Molecular Orbital Method","Amber MD","Interleukin-1ß"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["hdl:1920/11650"],"render_values":[{"text":"hdl:1920/11650","href":null,"code":true}]}]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Molecular dynamics","Fragment Molecular Orbital Method","Amber MD","Interleukin-1ß"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["hdl:1920/11650"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.other","label":"Dc Description Other","values":["Osteoarthritis affects millions of people worldwide each year. The inflammatory signaling pathway associated with osteoarthritis contains a possible novel drug target, the IL-1β ternary complex. IL-1β interacts with two associated proteins, IL-1RI and IL-1RAcP, to exert downstream inflammatory effects. Experimental studies of this complex have identified residue Arg-286 of IL-1RAcP as a “hot spot” of interaction. This paper aimed to computationally study the IL-1β complex with molecular mechanical and quantum mechanical methods. The study found Arg-286 of IL-1RAcP to be the hot spot, participating in a hydrogen bond with Asp-54 of IL- 1β. In agreement with previous experimental studies, Arg-286 was identified as a possible target for drug discovery aimed at inhibiting IL-1β complex and its ultimate downstream inflammatory effects."]},{"key":"dc:title","label":"Title","values":["Molecular Dynamics Simulations on the Interleukin-1β:Interleukin Receptor I:Interleukin-1 Receptor Accessory Protein Ternary Complex"]}]}],"canonical_facts":{"dc:description.other":["Osteoarthritis affects millions of people worldwide each year. The inflammatory signaling pathway associated with osteoarthritis contains a possible novel drug target, the IL-1β ternary complex. IL-1β interacts with two associated proteins, IL-1RI and IL-1RAcP, to exert downstream inflammatory effects. Experimental studies of this complex have identified residue Arg-286 of IL-1RAcP as a “hot spot” of interaction. This paper aimed to computationally study the IL-1β complex with molecular mechanical and quantum mechanical methods. The study found Arg-286 of IL-1RAcP to be the hot spot, participating in a hydrogen bond with Asp-54 of IL- 1β. In agreement with previous experimental studies, Arg-286 was identified as a possible target for drug discovery aimed at inhibiting IL-1β complex and its ultimate downstream inflammatory effects."],"dc:identifier":["hdl:1920/11650"],"dc:subject":["Molecular dynamics","Fragment Molecular Orbital Method","Amber MD","Interleukin-1ß"],"dc:title":["Molecular Dynamics Simulations on the Interleukin-1β:Interleukin Receptor I:Interleukin-1 Receptor Accessory Protein Ternary Complex"],"dc:type":["Thesis"]},"updated_at":"2026-07-27T19:51:52Z"}