Does the location of a mutation determine the ability to form amyloid fibrils?
Does the location of a mutation determine the ability to form amyloid fibrils?
复制标题
突变的位置是否决定了形成淀粉样原纤维的能力？
DOI：
10.1016/s0022-2836(02)00840-9
复制
发表时间：
2002
影响因子：
5.6
通讯作者：
Regan,Lynne
中科院分区：
文献类型：
--
作者：
Ramírez-Alvarado,Marina;Regan,Lynne
We have previously reported studies of fibril formation by a set of protein G B1 domain (β1) variants, with mutations located around the central parallel β-strands. In this study, we designed multiple mutations in the edge strands of β1 to create proteins with a stability range comparable to that of the set of central mutants. All the edge variants are able to form amyloid fibrils when they are incubated at their melting temperatures. This result suggests that overall protein stability is the key determinant for amyloid formation and not the specific location of destabilizing mutations. The edge strand and variants cross-seed with each other and with members of the central variant family. Interesting fibrillar morphology was observed in some cross-seeding cases and its implications for a better understanding of nucleation and elongation events are discussed.
