Mok S S, Sberna G, Heffernan D, Cappai R, Galatis D, Clarris H J, Sawyer W H, Beyreuther K, Masters C L, Small D H
Department of Pathology, The University of Melbourne, Parkville, Victoria, Australia.
FEBS Lett. 1997 Oct 6;415(3):303-7. doi: 10.1016/s0014-5793(97)01146-0.
Deletion mutagenesis studies have suggested that there are two domains within APP which bind heparan sulphate. These domains have been cloned and expressed in the yeast Pichia pastoris. Both recombinant proteins bound to heparin. One domain (APP316-447) was further characterised by binding studies with peptides encompassing this region. Peptides homologous to APP316-346 and APP416-447 were found to bind heparin. Circular dichroism studies show that APP416-447 shifted towards an alpha-helical conformation in the presence of heparin. This study suggests that heparin-binding domains may lie within regions high in alpha-helical structure.
缺失诱变研究表明，淀粉样前体蛋白（APP）内有两个与硫酸乙酰肝素结合的结构域。这些结构域已被克隆并在毕赤酵母中表达。两种重组蛋白均能与肝素结合。通过与包含该区域的肽进行结合研究，对其中一个结构域（APP316 - 447）进行了进一步表征。发现与APP316 - 346和APP416 - 447同源的肽能结合肝素。圆二色性研究表明，在肝素存在的情况下，APP416 - 447向α - 螺旋构象转变。该研究表明，肝素结合结构域可能位于α - 螺旋结构含量高的区域内。
