Template-based structure modeling of protein-protein interactions.
The structure of protein-protein complexes can be constructed by using the known structure of other protein complexes as a template. The complex structure templates are generally detected either by homology-based sequence alignments or, given the structure of monomer components, by structure-based comparisons. Critical improvements have been made in recent years by utilizing interface recognition and by recombining monomer and complex template libraries. Encouraging progress has also been witnessed in genome-wide applications of template-based modeling, with modeling accuracy comparable to high-throughput experimental data. Nevertheless, bottlenecks exist due to the incompleteness of the protein-protein complex structure library and the lack of methods for distant homologous template identification and full-length complex structure refinement.
Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Karolina út 29, Budapest 1113, Hungary.
Andras
A
Szilagyi
Department of Computational Medicine & Bioinformatics, The University of Michigan, 100 Washtenaw Avenue, 2035B, Ann Arbor, MI 48109-2218, USA; Department of Biological Chemistry, The University of Michigan, 100 Washtenaw Avenue, 2035B, Ann Arbor, MI 48109-2218, USA. Electronic address: zhng@umich.edu.
Yang
Y
Zhang
D000595:Amino Acid Sequence; D000818:Animals; D030562:Databases, Protein; D006801:Humans; D062105:Molecular Docking Simulation / Q000379:methods*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
D011506:Proteins