Structural Basis Of FAD Mutations Within The Transmembrane Domain Of APP
We will 1) solve the structure of APPTM and 2) correlate structural characteristics of APPTM with properties in amyloid beta production.
A transmembrane domain is a part of a protein that helps to anchor it into the correct locations in the cell so that it can perform its function. Dr. Chunyu Wang and collaborators aimed to define the structure of the transmembrane portion of the Amyloid Precursor Protein, called APPTM. Knowing the structure of APPTM will help to define how gamma‐secretase binds to and digests APP, which in turn will determine the ratio of toxic beta‐amyloid 42 fragments to the less toxic beta‐amyloid 40 fragments. These researchers successfully produced protein samples of a normal APPTM and an Alzheimer's disease (AD)‐causing mutant and have collected high quality structural data with a method called “solution nuclear magnetic resonance.” These data provide important insight into the basic mechanisms of beta-amyloid generation and AD.
First published on: April 14, 2009
Last modified on: April 12, 2011