SISYPHUS--structural alignments for proteins with non-trivial relationships.

ABSTRACT: With the increasing amount of structural data, the number of homologous protein structures bearing topological irregularities is steadily growing. These include proteins with circular permutations, segment-swapping, context-dependent folding or chameleon sequences that can adopt alternative secondary structures. Their non-trivial structural relationships are readily identified during expert analysis but their automatic identification using the existing computational tools still remains difficult or impossible. Such non-trivial cases of protein relationships are known to pose a problem to multiple alignment algorithms and to impede comparative modeling studies. They support a new emerging concept of evolutionary changeable protein fold, which creates practical difficulties for the hierarchi

SUBMITTER: Andreeva A 

PROVIDER: S-EPMC1635320 | biostudies-literature | 2007 Jan

REPOSITORIES: biostudies-literature