N- and C-terminal regions of the small heat shock protein IbpA from <i>Acholeplasma laidlawii</i> competitively govern its oligomerization pattern and chaperone-like activity
Liliya S. Chernova, Mikhail I. Bogachev, Vitaly Chasov, Innokentii E. Vishnyakov, Airat R. Kayumov
Abstract
The CTD provides fibrils (active form) formation. The NTD leads to globules formation and behaves as an intramolecular inhibitor of CTD. Their competition governs the equilibrium between either fibrills or globules regulating the <italic>Al</italic>IbpA activity.
Topics & Concepts
Chaperone (clinical)OligomerFibrilGlobular proteinChemistryBiophysicsHeat shock proteinProtein foldingProtein aggregationBiochemistryBiologyGeneMedicineOrganic chemistryPathologyHeat shock proteins researchProtein Structure and DynamicsEnzyme Structure and Function