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Literature summary for 5.6.1.6 extracted from

  • Krasilnikov, O.V.; Sabirov, R.Z.; Okada, Y.
    ATP hydrolysis-dependent asymmetry of the conformation of CFTR channel pore (2011), J. Physiol. Sci., 61, 267-278.
    View publication on PubMed
Search for more literature for 5.6.1.6

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + closed Cl- channel = ADP + phosphate + open Cl- channel the structure of the CFTR channel pore is highly asymmetric with a narrower extracellular entrance and a dilating conformational change of the extracellular entrance is associated with the channel transition to a nonhydrolytic, locked-open state Homo sapiens
a

Source Tissue

Source Tissue Comment Organism Textmining
HEK-293T cell
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 Homo sapiens
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Subunits

Subunits Comment Organism
More polyethylene glycols with a hydrodynamic radius smaller than 0.95 nm added from the intracellular side greatly suppress the inward unitary anionic conductance, whereas only molecules with hydrodynamic radius below 0.62 nm applied extracellularly are able to affect the outward unitary anionic currents. Larger molecules with hydrodynamic radius of 1.16-1.84 nm added from either side are completely excluded from the pore and have no significant effect on the single-channel conductance. The cut-off radius of the inner entrance of CFTR channel pore is 1.19 nm. The outer entrance is narrower with its cut-off radius of 0.70 nm and is dilated to about 0.93 nm when a non-hydrolyzable ATP analog, 5'-adenylylimidodiphosphate, is added to the intracellular solution Homo sapiens