Inward rectifying potassium channels

Monica Sala-Rabanal; Colin Nichols

doi:10.1201/b18027-26

Inward rectifying potassium channels

Monica Sala-Rabanal, Colin Nichols

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

3 Scopus citations

Abstract

Functional Kir channels are formed by the homomeric or heteromeric assembly of four subunits, each Kir subunit containing two membrane-spanning domains (TM1 and TM2), an extracellular pore-forming region (H5) that includes the selectivity lter, and cytosolic NH2-and COOH-termini that associate with each other to form a cytoplasmic domain that controls gating (Figure 18.2) (Nishida et al. 2007, Whorton and MacKinnon 2011).

Original language	English
Title of host publication	Handbook of Ion Channels
Publisher	CRC Press
Pages	241-260
Number of pages	20
ISBN (Electronic)	9781466551428
DOIs	https://doi.org/10.1201/b18027-26
State	Published - Jan 1 2015

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abstract = "Functional Kir channels are formed by the homomeric or heteromeric assembly of four subunits, each Kir subunit containing two membrane-spanning domains (TM1 and TM2), an extracellular pore-forming region (H5) that includes the selectivity lter, and cytosolic NH2-and COOH-termini that associate with each other to form a cytoplasmic domain that controls gating (Figure 18.2) (Nishida et al. 2007, Whorton and MacKinnon 2011).",

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AB - Functional Kir channels are formed by the homomeric or heteromeric assembly of four subunits, each Kir subunit containing two membrane-spanning domains (TM1 and TM2), an extracellular pore-forming region (H5) that includes the selectivity lter, and cytosolic NH2-and COOH-termini that associate with each other to form a cytoplasmic domain that controls gating (Figure 18.2) (Nishida et al. 2007, Whorton and MacKinnon 2011).

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Inward rectifying potassium channels

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