Detection and alignment of 3D domain swapping proteins using angle-distance image-based secondary structural matching techniques.

ABSTRACT: This work presents a novel detection method for three-dimensional domain swapping (DS), a mechanism for forming protein quaternary structures that can be visualized as if monomers had "opened" their "closed" structures and exchanged the opened portion to form intertwined oligomers. Since the first report of DS in the mid 1990s, an increasing number of identified cases has led to the postulation that DS might occur in a protein with an unconstrained terminus under appropriate conditions. DS may play important roles in the molecular evolution and functional regulation of proteins and the formation of depositions in Alzheimer's and prion diseases. Moreover, it is promising for designing auto-assembling biomaterials. Despite the increasing interest in DS, related bioinformatics methods are rar

SUBMITTER: Chu CH 

PROVIDER: S-EPMC2955075 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature