title: Protein design by fusion: implications for protein structure prediction and evolution.
abstract: Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions.
authors: Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22093, USA.
authors: Katarzyna
authors: K
authors: Skorupka
authors: Seong Kyu
authors: SK
authors: Han
authors: Hyun-Jun
authors: HJ
authors: Nam
authors: Sanguk
authors: S
authors: Kim
authors: Salem
authors: S
authors: Faham
mesh_terms: D029063:Aquifoliaceae / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D019143:Evolution, Molecular; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D015202:Protein Engineering; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D040681:Structural Homology, Protein
chemical_list: D010940:Plant Proteins; D011993:Recombinant Fusion Proteins
keywords: protein design; protein fusion; protein threading; structure prediction