Abstract:
:Gap junction channels mediate intercellular signalling that is crucial in tissue development, homeostasis and pathologic states such as cardiac arrhythmias, cancer and trauma. To explore the mechanism by which Ca(2+) blocks intercellular communication during tissue injury, we determined the X-ray crystal structures of the human Cx26 gap junction channel with and without bound Ca(2+). The two structures were nearly identical, ruling out both a large-scale structural change and a local steric constriction of the pore. Ca(2+) coordination sites reside at the interfaces between adjacent subunits, near the entrance to the extracellular gap, where local, side chain conformational rearrangements enable Ca(2+)chelation. Computational analysis revealed that Ca(2+)-binding generates a positive electrostatic barrier that substantially inhibits permeation of cations such as K(+) into the pore. Our results provide structural evidence for a unique mechanism of channel regulation: ionic conduction block via an electrostatic barrier rather than steric occlusion of the channel pore.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Bennett BC,Purdy MD,Baker KA,Acharya C,McIntire WE,Stevens RC,Zhang Q,Harris AL,Abagyan R,Yeager Mdoi
10.1038/ncomms9770subject
Has Abstractpub_date
2016-01-12 00:00:00pages
8770issn
2041-1723pii
ncomms9770journal_volume
7pub_type
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