Journal article

Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein

J Rossjohn, R Cappai, SC Feil, A Henry, WJ McKinstry, D Galatis, L Hesse, G Multhaup, K Beyreuther, CL Masters, MW Parker

NATURE STRUCTURAL BIOLOGY | NATURE AMERICA INC | Published : 1999

Abstract

Amyloid precursor protein (APP) plays a central role in Alzheimer disease. A proteolytic-breakdown product of APP, called beta-amyloid, is a major component of the diffuse and fibrillar deposits found in Alzheimer diseased brains. The normal physiological role of APP remains largely unknown despite much work. A knowledge of its function will not only provide insights into the genesis of the disease but may also prove vital in the development of an effective therapy. Here we describe the 1.8 A resolution crystal structure of the N-terminal, heparin-binding domain of APP (residues 28-123), which is responsible, among other things, for stimulation of neurite outgrowth. The structure reveals a h..

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