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

Cellular Physiology and Biochemistry

关键词: ICln;    Structure;    NMR;    Intrinsic disorder;   

DOI  :  10.1159/000335852

学科分类：分子生物学，细胞生物学和基因

来源: S Karger AG

【 摘 要 】

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.

【 授权许可】

CC BY-NC-ND