5E5V

Structure of amyloid forming peptide NFGAILS (residues 22-28) from Islet Amyloid Polypeptide

Summary for 5E5V

• Entry DOI: 10.2210/pdb5e5v/pdb
• Related: 5E5X 5E5Z 5E61
• Descriptor: NFGAILS (22-28) from islet amyloid polypeptide, synthesized (2 entities in total)
• Functional Keywords: amyloid-like protofibril, protein fibril, de novo protein, membrane protein
• Biological source: Homo sapiens
• Total number of polymer chains: 2
• Total formula weight: 1441.63

Authors

Soriaga, A.B.,Macdonald, R.,Sawaya, M.R.,Sangwan, S.,Eisenberg, D. (deposition date: 2015-10-09, release date: 2015-12-16, Last modification date: 2024-03-06)

Primary citation

Soriaga, A.B.,Sangwan, S.,Macdonald, R.,Sawaya, M.R.,Eisenberg, D.
Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.
J.Phys.Chem.B, 120:5810-5816, 2016

PubMed Abstract: Structural studies of amyloidogenic segments by X-ray crystallography have revealed a novel packing motif, consisting of out-of-register β sheets, which 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 additional evidence of out-of-register β sheets as a common structural motif in amyloid aggregates.

PubMed: 26629790
DOI: 10.1021/acs.jpcb.5b09981

Experimental method

X-RAY DIFFRACTION (1.24 Å)