Evolution of protein fold in the presence of functional constraints

@article{citeulike:800660, abstract = {The functional requirement to form and maintain the active site structure probably exerts a strong selective pressure on a protein to adopt just one stable and evolutionarily conserved fold. Nonetheless, new evidence suggests the likelihood of protein fold being neither physically nor biologically invariant. Alternative folds discovered in several proteins are composed of constant and variable parts. The latter display context-dependent conformations and a tendency to form new oligomeric interfaces. In turn, oligomerisation mediates fold evolution without loss of protein function. Gene duplication breaks down homo-oligomeric symmetry and relieves the pressure to maintain the local architecture of redundant active sites; this can lead to further structural changes.}, author = {Andreeva, Antonina and Murzin, Alexey G. }, booktitle = {Nucleic acids/Sequences and topology - Anna Marie Pyle and Jonathan Widom/Nick V Grishin and Sarah A Teichmann}, citeulike-article-id = {800660}, doi = {http://dx.doi.org/10.1016/j.sbi.2006.04.003}, journal = {Current Opinion in Structural Biology}, keywords = {protein\_evolution, protein\_function, protein\_structure, structure\_classification}, month = {June}, number = {3}, pages = {399--408}, posted-at = {2007-01-24 03:21:02}, priority = {3}, title = {Evolution of protein fold in the presence of functional constraints}, url = {http://dx.doi.org/10.1016/j.sbi.2006.04.003}, volume = {16}, year = {2006} }

TY - JOUR ID - citeulike:800660 L3 - citeulike-article-id:800660 N2 - The functional requirement to form and maintain the active site structure probably exerts a strong selective pressure on a protein to adopt just one stable and evolutionarily conserved fold. Nonetheless, new evidence suggests the likelihood of protein fold being neither physically nor biologically invariant. Alternative folds discovered in several proteins are composed of constant and variable parts. The latter display context-dependent conformations and a tendency to form new oligomeric interfaces. In turn, oligomerisation mediates fold evolution without loss of protein function. Gene duplication breaks down homo-oligomeric symmetry and relieves the pressure to maintain the local architecture of redundant active sites; this can lead to further structural changes. IS - 3 JF - Current Opinion in Structural Biology EP - 408 TI - Evolution of protein fold in the presence of functional constraints VL - 16 T2 - Nucleic acids/Sequences and topology - Anna Marie Pyle and Jonathan Widom/Nick V Grishin and Sarah A Teichmann SP - 399 KW - protein_evolution KW - protein_function KW - protein_structure KW - structure_classification AU - Andreeva, Antonina AU - Murzin, Alexey PY - 2006/06// UR - http://dx.doi.org/10.1016/j.sbi.2006.04.003 ER -