Topology independent structural matching discovers novel templates for protein interfaces | Zendy

Claudio Mirabello | Zendy; Björn Wallner | Zendy

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Topology independent structural matching discovers novel templates for protein interfaces

Author(s) -

Claudio Mirabello,

Björn Wallner

Publication year - 2018

Publication title -

bioinformatics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.599

H-Index - 390

eISSN - 1367-4811

pISSN - 1367-4803

DOI - 10.1093/bioinformatics/bty587

Subject(s) - template , interface (matter) , sequence (biology) , topology (electrical circuits) , computer science , function (biology) , matching (statistics) , surface (topology) , code (set theory) , protein structure , biological system , set (abstract data type) , chemistry , geometry , parallel computing , mathematics , biology , programming language , combinatorics , biochemistry , statistics , bubble , maximum bubble pressure method , evolutionary biology

Protein-protein interactions (PPI) are essential for the function of the cellular machinery. The rapid growth of protein-protein complexes with known 3D structures offers a unique opportunity to study PPI to gain crucial insights into protein function and the causes of many diseases. In particular, it would be extremely useful to compare interaction surfaces of monomers, as this would enable the pinpointing of potential interaction surfaces based solely on the monomer structure, without the need to predict the complete complex structure. While there are many structural alignment algorithms for individual proteins, very few have been developed for protein interfaces, and none that can align only the interface residues to other interfaces or surfaces of interacting monomer subunits in a topology independent (non-sequential) manner.

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