1MWP

N-TERMINAL DOMAIN OF THE AMYLOID PRECURSOR PROTEIN

1MWP の概要

• エントリーDOI: 10.2210/pdb1mwp/pdb
• 分子名称: AMYLOID A4 PROTEIN (2 entities in total)
• 機能のキーワード: heparin binding, sugar binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P05067
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11051.76

構造登録者

Rossjohn, J.,Cappai, R.,Feil, S.C.,Henry, A.,McKinstry, W.J.,Galatis, D.,Hesse, L.,Multhaup, G.,Beyreuther, K.,Masters, C.L.,Parker, M.W. (登録日: 1999-03-09, 公開日: 2000-03-15, 最終更新日: 2024-10-30)

主引用文献

Rossjohn, J.,Cappai, R.,Feil, S.C.,Henry, A.,McKinstry, W.J.,Galatis, D.,Hesse, L.,Multhaup, G.,Beyreuther, K.,Masters, C.L.,Parker, M.W.
Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein.
Nat.Struct.Biol., 6:327-331, 1999

PubMed 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 highly charged basic surface that may interact with glycosaminoglycans in the brain and an abutting hydrophobic surface that is proposed to play an important functional role such as dimerization or ligand binding. Structural similarities with cysteine-rich growth factors, taken together with its known growth-promoting properties, suggests the APP N-terminal domain could function as a growth factor in vivo.

PubMed: 10201399
DOI: 10.1038/7562

実験手法

X-RAY DIFFRACTION (1.8 Å)