Structural highlights
Publication Abstract from PubMed
Structural studies of amyloidogenic segments by X-ray crystallography have revealed a novel packing motif, consisting of out-of-register beta sheets, that may constitute one of the toxic species in aggregation related diseases. Here we sought to determine the presence of such a motif in Islet amyloid polypeptide (IAPP), whose amyloidogenic properties are associated with Type 2 Diabetes. We determined four new crystal structures of segments within IAPP all forming steric zippers. Most interestingly, one of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. Our results provide evidence that out-of-register beta sheets may be a common structural motif in amyloid aggregates and may be associated with toxicity.
Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.,Soriaga AB, Sangwan S, Macdonald R, Sawaya MR, Eisenberg D J Phys Chem B. 2015 Dec 2. PMID:26629790[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Soriaga AB, Sangwan S, Macdonald R, Sawaya MR, Eisenberg D. Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets. J Phys Chem B. 2015 Dec 2. PMID:26629790 doi:http://dx.doi.org/10.1021/acs.jpcb.5b09981
