title: The C-terminus of ICln is natively disordered but displays local structural preformation.
abstract: ICln is a vital, ubiquitously expressed protein with roles in cell volume regulation, angiogenesis, cell morphology, activation of platelets and RNA processing. In previous work we have determined the 3D structure of the N-terminus of ICln (residues 1-159), which folds into a PH-like domain followed by an unstructured region (residues H134 - Q159) containing protein-protein interaction sites. Here we present sequence-specific resonance assignments of the C-terminus (residues Q159 - H235) of ICln by NMR, and show that this region of the protein is intrinsically unstructured. By applying (13)Cα- (13)Cβ secondary chemical shifts to detect possible preferences for secondary structure elements we show that the C-terminus of ICln adopts a preferred α-helical organization between residues E170 and E187, and exists preferentially in extended conformations (β-strands) between residues D161 to Y168 and E217 to T223.
authors.affiliation: Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
authors.forename: Andreas
authors.initials: A
authors.lastname: Schedlbauer
authors.forename: Rosaria
authors.initials: R
authors.lastname: Gandini
authors.forename: Georg
authors.initials: G
authors.lastname: Kontaxis
authors.forename: Markus
authors.initials: M
authors.lastname: Paulmichl
authors.forename: Johannes
authors.initials: J
authors.lastname: Furst
authors.forename: Robert
authors.initials: R
authors.lastname: Konrat
mesh_terms: D000818:Animals; D018118:Chloride Channels / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004285:Dogs; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D018118:Chloride Channels; D011994:Recombinant Proteins