Journal article

The crystal structure of amyloid precursor-like protein 2 E2 domain completes the amyloid precursor protein family

Laila C Roisman, Sen Han, Mun Joo Chuei, Andrea R Connor, Roberto Cappai

FASEB JOURNAL | FEDERATION AMER SOC EXP BIOL | Published : 2019

Abstract

The amyloid precursor-like protein 2 (APLP2) molecule is a type I transmembrane protein that is crucial for survival, cell-cell adhesion, neuronal development, myelination, cancer metastasis, modulation of metal, and glucose and insulin homeostasis. Moreover, the importance of the amyloid precursor protein (APP) family in biology and disease is very well known because of its central role in Alzheimer disease. In this study, we determined the crystal structure of the independently folded E2 domain of APLP2 and compared that with its paralogues APP and APLP2, demonstrating high overall structural similarities. The crystal structure of APLP2 E2 was solved as an antiparallel dimer, and analysis ..

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Grants

Funding Acknowledgements

The authors thank the Australian Synchrotron, especially the staff at the MX2 Beamline, for friendly and helpful assistance with data collection; Dr. Zhiguang Xiao (Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne), for helpful review of the manuscript; and Nathan Gerstman for helpful visual crystal screening. This work was supported by funding from the National Health and Medical Research Council of Australia (to R.C). The authors declare no conflicts of interest.