KUO-LONG LOUChou, Hsiu ChuanHsiu ChuanChouTsai, Yau WeiYau WeiTsaiShiau, Yu ShuanYu ShuanShiauHuang, Po TsangPo TsangHuangChen, Ting YuTing YuChenShiau, Yuh YuanYuh YuanShiauFrench, Robert J.Robert J.French2024-01-252024-01-252001-12-0116102940https://scholars.lib.ntu.edu.tw/handle/123456789/638886Rundown is a generally encountered problem while recording KATP channel activity with inside-out patches. No assigned structural fragment related to this mechanism has yet been derived from any of the functional analyses performed. Therefore, based on a combined sequence and secondary structure alignment against known crystal structure of segments from closely related proteins, we propose here the three-dimensional structural model of an intracellular C-terminal domain of the Kir6.2 subunit in KATP channels. An E. coli CMP-kinase was suggested as template for the model building. The subdomain arrangement of this novel kinase domain and the structural correlation for UDP-docking are described. With structural-functional interpretation, we conclude that the reactivation of KATP channel rundown by MgATP or UDP is very possibly regulated by this intracellular kinase domain at the C-terminus of Kir6.2 subunit in KATP channels.3D homology modeling | Channel gating | Kinase domain | Kir6.2 | Rundown reactivationjournal article10.1007/S0089401000102-s2.0-0035789538https://api.elsevier.com/content/abstract/scopus_id/0035789538