Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

Christine Röder; Nicola Vettore; Lena N. Mangels; Lothar Gremer; Raimond B. G. Ravelli; Dieter Willbold; Wolfgang Hoyer; Alexander K. Buell; Gunnar F. Schröder

doi:10.1038/s41467-019-11320-8

Nature Communications (Aug 2019)

Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy

Christine Röder,
Nicola Vettore,
Lena N. Mangels,
Lothar Gremer,
Raimond B. G. Ravelli,
Dieter Willbold,
Wolfgang Hoyer,
Alexander K. Buell,
Gunnar F. Schröder

Affiliations

Christine Röder: Institute of Complex Systems, Structural Biochemistry (ICS-6) and JuStruct, Jülich Center for Structural Biology, Forschungszentrum Jülich
Nicola Vettore: Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf
Lena N. Mangels: Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf
Lothar Gremer: Institute of Complex Systems, Structural Biochemistry (ICS-6) and JuStruct, Jülich Center for Structural Biology, Forschungszentrum Jülich
Raimond B. G. Ravelli: The Maastricht Multimodal Molecular Imaging Institute, Maastricht University
Dieter Willbold: Institute of Complex Systems, Structural Biochemistry (ICS-6) and JuStruct, Jülich Center for Structural Biology, Forschungszentrum Jülich
Wolfgang Hoyer: Institute of Complex Systems, Structural Biochemistry (ICS-6) and JuStruct, Jülich Center for Structural Biology, Forschungszentrum Jülich
Alexander K. Buell: Institut für Physikalische Biologie, Heinrich-Heine-Universität Düsseldorf
Gunnar F. Schröder: Institute of Complex Systems, Structural Biochemistry (ICS-6) and JuStruct, Jülich Center for Structural Biology, Forschungszentrum Jülich

DOI: https://doi.org/10.1038/s41467-019-11320-8
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 9

Abstract

Read online

The Src-homology 3 domain of phosphatidyl-inositol-3-kinase (PI3K-SH3) is a model system for studying amyloid fibril formation. Here the authors present the 3.4 Å cryo-EM structure of the PI3K-SH3 amyloid fibril, which allows them to rationalize the effects of mutations on the kinetics of fibril formation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

About the journal