The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation

Andreas Schedlbauer, Rosaria Gandini, Georg Kontaxis, Markus Paulmichl, Johannes Furst, Robert Konrat

Veröffentlichungen: Beitrag in FachzeitschriftArtikelPeer Reviewed


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)C alpha-(13)C beta secondary chemical shifts to detect possible preferences for secondary structure elements we show that the C-terminus of ICln adopts a preferred a-helical organization between residues E170 and E187, and exists preferentially in extended conformations (beta-strands) between residues D161 to Y168 and E217 to T223.
Seiten (von - bis)1203-1210
FachzeitschriftCellular Physiology and Biochemistry
PublikationsstatusVeröffentlicht - 2011

ÖFOS 2012

  • 106002 Biochemie