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TitleA new polymorphism of human amylin fibrils with similar protofilaments and a conserved core.
Journal, issue, pagesiScience, Vol. 25, Issue 12, Page 105705, Year 2022
Publish dateDec 22, 2022
AuthorsDongyu Li / Xueli Zhang / Youwang Wang / Haonan Zhang / Kai Song / Keyan Bao / Ping Zhu /
PubMed AbstractPancreatic amyloid deposits composed of a fibrillar form of the human islet amyloid polypeptide (hIAPP) are the pathological hallmark of type 2 diabetes (T2D). Although various cryo-EM structures of ...Pancreatic amyloid deposits composed of a fibrillar form of the human islet amyloid polypeptide (hIAPP) are the pathological hallmark of type 2 diabetes (T2D). Although various cryo-EM structures of polymorphic hIAPP fibrils were reported, the underlying polymorphic mechanism of hIAPP remains elusive. Meanwhile, the structure of hIAPP fibrils with all residues visible in the fibril core is not available. Here, we report the full-length structures of two different polymorphs of hIAPP fibrils, namely slim form (SF, dimer) and thick form (TF, tetramer), formed in a salt-free environment, which share a similar ζ-shaped protofilament but differ in inter-protofilament interfaces. In the absence of salt, electrostatic interactions were found to play a dominant role in stabilizing the fibril structure, suggesting an antagonistic effect between electrostatic and hydrophobic interactions in different salt concentrations environments. Our results shed light on understanding the mechanism of amyloid fibril polymorphism.
External linksiScience / PubMed:36567711 / PubMed Central
MethodsEM (helical sym.)
Resolution3.2 - 3.6 Å
Structure data

33897

7ykw

EMDB-33897, PDB-7ykw:
Structure of hIAPP fibril at 3.6 Angstroms resolution
Method: EM (helical sym.) / Resolution: 3.6 Å

33901

7yl0

EMDB-33901, PDB-7yl0:
Structure of hIAPP-TF-type2
Method: EM (helical sym.) / Resolution: 3.2 Å

33902

7yl3

EMDB-33902, PDB-7yl3:
Structure of hIAPP-TF-type1
Method: EM (helical sym.) / Resolution: 3.2 Å

33903

7yl7

EMDB-33903, PDB-7yl7:
Structure of hIAPP-TF-type3
Method: EM (helical sym.) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
KeywordsPROTEIN FIBRIL / amylin / hIAPP

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