Ontology highlight
ABSTRACT:
SUBMITTER: Dahms SO
PROVIDER: S-EPMC2851805 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
Dahms Sven O SO Hoefgen Sandra S Roeser Dirk D Schlott Bernhard B Gührs Karl-Heinz KH Than Manuel E ME
Proceedings of the National Academy of Sciences of the United States of America 20100308 12
The amyloid precursor protein (APP) is the key player in Alzheimer's disease pathology, yet APP and its analogues are also essential for neuronal development and cell homeostasis in mammals. We have determined the crystal structure of the entire N-terminal APP-E1 domain consisting of the growth factor like and the copper binding domains at 2.7-A resolution and show that E1 functions as a rigid functional entity. The two subdomains interact tightly in a pH-dependent manner via an evolutionarily c ...[more]