1s1g

File:1s1g.jpg

spinqualitylabelsall models 1s1g, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Kv4.3 T1 Domain

OverviewOverview

The family of calcium binding proteins called KChIPs associates with Kv4, family K(+) channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction, between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7-11 and 71-90, are necessary for KChIP1 modulation and, interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues, 71-90 of Kv4.2 are also sufficient to confer association with KChIP1. To, provide a structural framework for these data, we solved the crystal, structures of Kv4.3N and KChIP1 individually. Taken together with the, mutagenesis data, the individual structures suggest that that the Kv4 N, terminus is required for stable association with KChIP1, perhaps through a, hydrophobic surface interaction, and that residues 71-90 in Kv4 subunits, form a contact loop that mediates the specific association of KChIPs with, Kv4 subunits.

About this StructureAbout this Structure

1S1G is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1., Scannevin RH, Wang K, Jow F, Megules J, Kopsco DC, Edris W, Carroll KC, Lu Q, Xu W, Xu Z, Katz AH, Olland S, Lin L, Taylor M, Stahl M, Malakian K, Somers W, Mosyak L, Bowlby MR, Chanda P, Rhodes KJ, Neuron. 2004 Feb 19;41(4):587-98. PMID:14980207

Page seeded by OCA on Fri Feb 15 16:51:23 2008