Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.
作者： Marcin I. Apostol , Kay Perry , Witold K. Surewicz
DOI: 10.1021/JA403001Q
关键词: Crystal structure 、 Chemistry 、 Zipper 、 Structural motif 、 Protein structure 、 Protein aggregation 、 Crystallography 、 Oligomer 、 Stereochemistry 、 Steric effects 、 Gene isoform
摘要: The structural transition of the prion protein from α-helical- to β-sheet-rich underlies its conversion into infectious and disease-associated isoforms. Here we describe crystal structure a fragment human consisting disulfide-bond-linked portions helices 2 3. Instead forming pair-of-sheets steric zipper characteristic amyloid fibers, this crystallized assembly hexameric oligomers. This study reveals never before observed motif for ordered aggregates suggests possible mechanism self-propagation misfolded conformations by such nonamyloid
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