We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Glycine 384 is required for presenilin-1 function and is conserved in bacterial polytopic aspartyl proteases.
- Authors
Steiner, H; Kostka, M; Romig, H; Basset, G; Pesold, B; Hardy, J; Capell, A; Meyn, L; Grim, M L; Baumeister, R; Fechteler, K; Haass, C
- Abstract
Endoproteolysis of beta-amyloid precursor protein (betaAPP) and Notch requires conserved aspartate residues in presenilins 1 and 2 (PS1 and PS2). Although PS1 and PS2 have therefore been proposed to be aspartyl proteases, no homology to other aspartyl proteases has been found. Here we identify homology between the presenilin active site and polytopic aspartyl proteases of bacterial origin, thus supporting the hypothesis that presenilins are novel aspartyl proteases.
- Publication
Nature cell biology, 2000, Vol 2, Issue 11, p848
- ISSN
1465-7392
- Publication type
Journal Article
- DOI
10.1038/35041097