Intramolecular Interaction of SUR2 Subtypes for Intracellular ADP-Induced Differential Control of KATP Channels
ATP-sensitive K (KATP) channels are composed of sulfonylurea receptors (SURs) and inwardly rectifying Kir6.2-channels. The C-terminal 42 amino acid residues (C42) of SURs are responsible for ADP-induced differential activation of KATP channels in SUR-subtypes. By examining ADP-effect on KATP channel...
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Published in | Circulation research Vol. 90; no. 5; pp. 554 - 561 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Hagerstown, MD
American Heart Association, Inc
22.03.2002
Lippincott |
Subjects | |
Online Access | Get full text |
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Summary: | ATP-sensitive K (KATP) channels are composed of sulfonylurea receptors (SURs) and inwardly rectifying Kir6.2-channels. The C-terminal 42 amino acid residues (C42) of SURs are responsible for ADP-induced differential activation of KATP channels in SUR-subtypes. By examining ADP-effect on KATP channels containing various chimeras of SUR2A and SUR2B, we identified a segment of 7 residues at central portion of C42 critical for this phenomenon. A 3-D structure model of the region containing the second nucleotide-binding domain (NBD2) of SUR and C42 was developed based on the structure of HisP, a nucleotide-binding protein forming the bacterial Histidine transporter complex. In the model, the polar and charged residues in the critical segment located within a distance that allows their electrostatic interaction with Arg1344 at the Walker-A loop of NBD2. Therefore, the interaction might be involved in the control of ADP-induced differential activation of SUR2-subtype KATP channels. |
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ISSN: | 0009-7330 1524-4571 |
DOI: | 10.1161/01.RES.0000012666.42782.30 |