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Apolipoprotein A‐I: the dual face of a protein
Author(s) -
Arciello Angela,
Piccoli Renata,
Monti Daria Maria
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12468
Subject(s) - apolipoprotein b , dimer , chemistry , monomer , fibril , amyloidosis , point mutation , lipid metabolism , flexibility (engineering) , amyloid (mycology) , mutation , biochemistry , biophysics , computational biology , biology , medicine , gene , cholesterol , inorganic chemistry , statistics , mathematics , organic chemistry , polymer
Conformational plasticity and flexibility are key structural features of Apo AI in lipid metabolism. Amyloidogenic single point mutations, associated with incurable familial amyloidosis with fibril deposition in peripheral organs, may have a dramatic impact on the structural and functional features of Apo AI . Here, the consistent body of data on Apo AI variants has been reviewed, with the aim of highlighting the hallmarks of the pathology. In accordance with our observations, as well as that of others, we propose a model that accounts for the alteration of the delicate balance between lipid‐free/lipid‐bound dynamic states which is based on monomer‐to‐dimer interconversion via domain swapping.