樓國隆Lou, Kuo-LongKuo-LongLou2006-07-262018-07-092006-07-262018-07-092000http://ntur.lib.ntu.edu.tw//handle/246246/22654Rundown is a generally encountered problem while recording KATP channel activity with inside-out patches. No assigned structural fragment related to this mechanism could be derived from any of the proceeded functional analyses as yet. 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 structure 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 were 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 Cterminus of Kir6.2 subunit in KATP channels.application/pdf50050 bytesapplication/pdfzh-TW國立臺灣大學醫學院口腔生物科學研究所Channel gating3-D homology modellingKinase domainjournal articlehttp://ntur.lib.ntu.edu.tw/bitstream/246246/22654/1/892314B002258.pdf