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TitleFibril structures of diabetes-related amylin variants reveal a basis for surface-templated assembly.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 11, Page 1048-1056, Year 2020
Publish dateSep 14, 2020
AuthorsRodrigo Gallardo / Matthew G Iadanza / Yong Xu / George R Heath / Richard Foster / Sheena E Radford / Neil A Ranson /
PubMed AbstractAggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G ...Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been established, the S20G mutation in amylin is associated with early-onset T2D. Here we report cryo-EM structures of amyloid fibrils of wild-type human amylin and its S20G variant. The wild-type fibril structure, solved to 3.6-Å resolution, contains two protofilaments, each built from S-shaped subunits. S20G fibrils, by contrast, contain two major polymorphs. Their structures, solved at 3.9-Å and 4.0-Å resolution, respectively, share a common two-protofilament core that is distinct from the wild-type structure. Remarkably, one polymorph contains a third subunit with another, distinct, cross-β conformation. The presence of two different backbone conformations within the same fibril may explain the increased aggregation propensity of S20G, and illustrates a potential structural basis for surface-templated fibril assembly.
External linksNat Struct Mol Biol / PubMed:32929282
MethodsEM (helical sym.)
Resolution3.6 - 4.0 Å
Structure data

11380

6zrf

EMDB-11380, PDB-6zrf:
amyloid structure of amylin (IAPP - islet amyloid polypeptide)
Method: EM (helical sym.) / Resolution: 3.6 Å

11382

6zrq

EMDB-11382, PDB-6zrq:
two-protofilament amyloid structure of S20G variant of human amylin (IAPP - islet amyloid polypeptide)
Method: EM (helical sym.) / Resolution: 3.9 Å

11383

6zrr

EMDB-11383, PDB-6zrr:
three-protofilament amyloid structure of S20G variant of human amylin (IAPP - Islet Amyloid Polypeptide)
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • synthetic construct (others)
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amyloid fibril type-2-diabetes hormone / amyloid fibril type-2-diabetes early-onset

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