1S1E

Crystal Structure of Kv Channel-interacting protein 1 (KChIP-1)

Summary for 1S1E

• Entry DOI: 10.2210/pdb1s1e/pdb
• Descriptor: Kv channel interacting protein 1, CALCIUM ION (3 entities in total)
• Functional Keywords: kchip, kv channel-interacting protein, calcium-binding protein, ef-finger, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Peripheral membrane protein (By similarity): Q9NZI2
• Total number of polymer chains: 1
• Total formula weight: 26424.98

Authors

Scannevin, R.H.,Wang, K.-W.,Jow, F.,Megules, J.,Kopsco, D.C.,Edris, W.,Carroll, K.C.,Lu, Q.,Xu, W.-X.,Xu, Z.-B.,Katz, A.H.,Olland, S.,Lin, L.,Taylor, M.,Stahl, M.,Malakian, K.,Somers, W.,Mosyak, L.,Bowlby, M.R.,Chanda, P.,Rhodes, K.J. (deposition date: 2004-01-06, release date: 2005-01-11, Last modification date: 2023-08-23)

Primary citation

Scannevin, R.H.,Wang, K.-W.,Jow, F.,Megules, J.,Kopsco, D.C.,Edris, W.,Carroll, K.C.,Xu, W.-X.,Xu, Z.-B.,Katz, A.H.,Olland, S.,Lin, L.,Taylor, M.,Stahl, M.,Malakian, K.,Somers, W.,Mosyak, L.,Bowlby, M.R.,Chanda, P.,Rhodes, K.J.
Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1.
Neuron, 41:587-598, 2004

PubMed Abstract: 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.

PubMed: 14980207
DOI: 10.1016/S0896-6273(04)00049-2

Experimental method

X-RAY DIFFRACTION (2.3 Å)