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TitleAtomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy.
Journal, issue, pagesNat Commun, Vol. 10, Issue 1, Page 3754, Year 2019
Publish dateAug 21, 2019
AuthorsChristine Röder / Nicola Vettore / Lena N Mangels / Lothar Gremer / Raimond B G Ravelli / Dieter Willbold / Wolfgang Hoyer / Alexander K Buell / Gunnar F Schröder /
PubMed AbstractHigh resolution structural information on amyloid fibrils is crucial for the understanding of their formation mechanisms and for the rational design of amyloid inhibitors in the context of protein ...High resolution structural information on amyloid fibrils is crucial for the understanding of their formation mechanisms and for the rational design of amyloid inhibitors in the context of protein misfolding diseases. The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model amyloid system that plays a pivotal role in our basic understanding of protein misfolding and aggregation. Here, we present the atomic model of the PI3K-SH3 amyloid fibril with a resolution determined to 3.4 Å by cryo-electron microscopy (cryo-EM). The fibril is composed of two intertwined protofilaments that create an interface spanning 13 residues from each monomer. The model comprises residues 1-77 out of 86 amino acids in total, with the missing residues located in the highly flexible C-terminus. The fibril structure allows us to rationalise the effects of chemically conservative point mutations as well as of the previously reported sequence perturbations on PI3K-SH3 fibril formation and growth.
External linksNat Commun / PubMed:31434882 / PubMed Central
MethodsEM (helical sym.)
Resolution3.4 Å
Structure data

4727

6r4r

EMDB-4727, PDB-6r4r:
Cryo-EM Structure of the PI3-Kinase SH3 Domain Amyloid Fibril
Method: EM (helical sym.) / Resolution: 3.4 Å

Source
  • bos taurus (cattle)
KeywordsPROTEIN FIBRIL / amyloid fibril / sh3 domain

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