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The C-terminus of ICln is natively disordered but displays local structural preformation

Andreas Schedlbauer1, Rosaria Gandini, Georg Kontaxis

  • 1Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.

Cellular Physiology and Biochemistry : International Journal of Experimental Cellular Physiology, Biochemistry, and Pharmacology
|December 20, 2011
PubMed

Insights

The C-terminus of ICln (Intracellular决赛) is intrinsically unstructured but shows preferences for alpha-helical and beta-strand formations. This finding provides insights into ICln protein structure and function.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • ICln (Intracellular决赛) is a crucial protein involved in diverse cellular processes including cell volume regulation, angiogenesis, and RNA processing.
  • Previous studies elucidated the N-terminus structure, revealing a PH-like domain and an unstructured region with interaction sites.

Purpose of the Study:

  • To determine the structural characteristics of the C-terminus of ICln (residues Q159-H235).
  • To investigate the secondary structure preferences within the intrinsically unstructured C-terminal region.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed for sequence-specific resonance assignments.
  • (13)Cα-(13)Cβ secondary chemical shifts were analyzed to identify secondary structure propensities.

Main Results:

  • The C-terminus of ICln (residues Q159-H235) was confirmed to be intrinsically unstructured.
  • Specific regions within the C-terminus exhibit preferences for secondary structures: alpha-helical organization (E170-E187) and extended conformations/beta-strands (D161-Y168 and E217-T223).

Conclusions:

  • The C-terminus of ICln, while largely unstructured, possesses localized secondary structure preferences.
  • These findings contribute to a more comprehensive understanding of ICln's overall structure-function relationship.

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