7sit

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Crystal structure of Voltage gated potassium ion channel, Kv 1.2 chimera-3m

Structural highlights

7sit is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.32Å
Ligands:K, NAP, O
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCAB2_RAT Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.

Publication Abstract from PubMed

C-type inactivation is a process by which ion flux through a voltage-gated K(+) (K(v)) channel is regulated at the selectivity filter. While prior studies have indicated that C-type inactivation involves structural changes at the selectivity filter, the nature of the changes has not been resolved. Here, we report the crystal structure of the K(v)1.2 channel in a C-type inactivated state. The structure shows that C-type inactivation involves changes in the selectivity filter that disrupt the outer two ion binding sites in the filter. The changes at the selectivity filter propagate to the extracellular mouth and the turret regions of the channel pore. The structural changes observed are consistent with the functional hallmarks of C-type inactivation. This study highlights the intricate interplay between K(+) occupancy at the ion binding sites and the interactions of the selectivity filter in determining the balance between the conductive and the inactivated conformations of the filter.

Structural basis for C-type inactivation in a Shaker family voltage-gated K(+) channel.,Reddi R, Matulef K, Riederer EA, Whorton MR, Valiyaveetil FI Sci Adv. 2022 Apr 22;8(16):eabm8804. doi: 10.1126/sciadv.abm8804. Epub 2022 Apr , 22. PMID:35452285[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. Reddi R, Matulef K, Riederer EA, Whorton MR, Valiyaveetil FI. Structural basis for C-type inactivation in a Shaker family voltage-gated K(+) channel. Sci Adv. 2022 Apr 22;8(16):eabm8804. PMID:35452285 doi:10.1126/sciadv.abm8804

Contents


PDB ID 7sit

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