3OR6

On the structural basis of modal gating behavior in K+channels - E71Q

Summary for 3OR6

• Entry DOI: 10.2210/pdb3or6/pdb
• Related: 3OR7
• Descriptor: antibody fab fragment heavy chain, antibody fab fragment light chain, Voltage-gated potassium channel, ... (5 entities in total)
• Functional Keywords: inactivation, alpha-helical, potassium channel, immune system-transport protein complex, immune system/transport protein
• Biological source: Streptomyces lividans; More
• Total number of polymer chains: 3
• Total formula weight: 58098.42

Authors

Chakrapani, S.,Cordero-Morales, J.F.,Jogini, V.,Perozo, E. (deposition date: 2010-09-06, release date: 2011-01-05, Last modification date: 2018-08-29)

Primary citation

Chakrapani, S.,Cordero-Morales, J.F.,Jogini, V.,Pan, A.C.,Cortes, D.M.,Roux, B.,Perozo, E.
On the structural basis of modal gating behavior in K(+) channels.
Nat.Struct.Mol.Biol., 18:67-74, 2011

PubMed Abstract: Modal-gating shifts represent an effective regulatory mechanism by which ion channels control the extent and time course of ionic fluxes. Under steady-state conditions, the K(+) channel KcsA shows three distinct gating modes, high-P(o), low-P(o) and a high-frequency flicker mode, each with about an order of magnitude difference in their mean open times. Here we show that in the absence of C-type inactivation, mutations at the pore-helix position Glu71 unmask a series of kinetically distinct modes of gating in a side chain-specific way. These gating modes mirror those seen in wild-type channels and suggest that specific interactions in the side chain network surrounding the selectivity filter, in concert with ion occupancy, alter the relative stability of pre-existing conformational states of the pore. The present results highlight the key role of the selectivity filter in regulating modal gating behavior in K(+) channels.

PubMed: 21186363
DOI: 10.1038/nsmb.1968

Experimental method

X-RAY DIFFRACTION (2.7 Å)