2i2r

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Crystal structure of the KChIP1/Kv4.3 T1 complexCrystal structure of the KChIP1/Kv4.3 T1 complex

Structural highlights

2i2r is a 16 chain structure with sequence from Buffalo rat and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:Kcnd3 (Buffalo rat), KCNIP1, KCHIP1, VABP (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[KCND3_RAT] Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.[1] [2] [3] [4] [KCIP1_HUMAN] Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND1/Kv4.1 and KCND2/Kv4.2 currents. Seems to be involved in KCND2 trafficking to the cell surface.[5] [6] [7]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function.

Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer.,Pioletti M, Findeisen F, Hura GL, Minor DL Jr Nat Struct Mol Biol. 2006 Nov;13(11):987-95. Epub 2006 Oct 22. PMID:17057713[8]

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

See Also

References

  1. ↑ Dixon JE, Shi W, Wang HS, McDonald C, Yu H, Wymore RS, Cohen IS, McKinnon D. Role of the Kv4.3 K+ channel in ventricular muscle. A molecular correlate for the transient outward current. Circ Res. 1996 Oct;79(4):659-68. PMID:8831489
  2. ↑ Serodio P, Vega-Saenz de Miera E, Rudy B. Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain. J Neurophysiol. 1996 May;75(5):2174-9. PMID:8734615
  3. ↑ Tsaur ML, Chou CC, Shih YH, Wang HL. Cloning, expression and CNS distribution of Kv4.3, an A-type K+ channel alpha subunit. FEBS Lett. 1997 Jan 3;400(2):215-20. PMID:9001401
  4. ↑ Ohya S, Tanaka M, Oku T, Asai Y, Watanabe M, Giles WR, Imaizumi Y. Molecular cloning and tissue distribution of an alternatively spliced variant of an A-type K+ channel alpha-subunit, Kv4.3 in the rat. FEBS Lett. 1997 Dec 22;420(1):47-53. PMID:9450548
  5. ↑ An WF, Bowlby MR, Betty M, Cao J, Ling HP, Mendoza G, Hinson JW, Mattsson KI, Strassle BW, Trimmer JS, Rhodes KJ. Modulation of A-type potassium channels by a family of calcium sensors. Nature. 2000 Feb 3;403(6769):553-6. PMID:10676964 doi:10.1038/35000592
  6. ↑ Nakamura TY, Nandi S, Pountney DJ, Artman M, Rudy B, Coetzee WA. Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4 subfamily members, Kv4.1 and Kv4.2. FEBS Lett. 2001 Jun 22;499(3):205-9. PMID:11423117
  7. ↑ Shibata R, Misonou H, Campomanes CR, Anderson AE, Schrader LA, Doliveira LC, Carroll KI, Sweatt JD, Rhodes KJ, Trimmer JS. A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels. J Biol Chem. 2003 Sep 19;278(38):36445-54. Epub 2003 Jun 26. PMID:12829703 doi:10.1074/jbc.M306142200
  8. ↑ Pioletti M, Findeisen F, Hura GL, Minor DL Jr. Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer. Nat Struct Mol Biol. 2006 Nov;13(11):987-95. Epub 2006 Oct 22. PMID:17057713 doi:10.1038/nsmb1164

2i2r, resolution 3.35Å

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