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- Title
The C-terminus of ICln is Natively Disordered but Displays Local Structural Preformation.
- Authors
Schedlbauer, Andreas; Gandini, Rosaria; Kontaxis, Georg; Paulmichl, Markus; Furst, Johannes; Konrat, Robert
- 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 13Cα- 13Cβ 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. Copyright © 2011 S. Karger AG, Basel
- Subjects
CELLULAR control mechanisms; NEOVASCULARIZATION; CELL culture; BLOOD platelets; MOLECULAR structure; PROTEIN-protein interactions; RNA
- Publication
Cellular Physiology & Biochemistry (Karger AG), 2011, Vol 28, Issue 6, p1203
- ISSN
1015-8987
- Publication type
Article
- DOI
10.1159/000335852