Can correlated mutations in protein domain families be used for protein design? Export

@article{citeulike:3111897, abstract = {Evidence from diverse studies, such as protein design experiments and analysis of the emergence of drug resistance in human immunodeficiency virus 1 (HIV-1), indicates that protein function can be diminished or altered by mutations at positions distant from the classic functional' site. Furthermore, results from correlation analysis of the ligand-binding domain of nuclear receptors suggest that mutation events at positions distributed throughout a protein domain may be involved in functional diversification during the evolution of homologous domain families. This review explores potential applications for a protein design procedure based on correlated substitutions. 10.1093/bib/2.3.279}, author = {Nagl, Sylvia B.}, citeulike-article-id = {3111897}, citeulike-linkout-0 = {http://dx.doi.org/10.1093/bib/2.3.279}, citeulike-linkout-1 = {http://bib.oxfordjournals.org/cgi/content/abstract/2/3/279}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/11589588}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=11589588}, day = {1}, doi = {10.1093/bib/2.3.279}, journal = {Brief Bioinform}, keywords = {correlated\_mutations}, month = {January}, number = {3}, pages = {279--288}, posted-at = {2008-08-19 09:28:52}, priority = {2}, title = {Can correlated mutations in protein domain families be used for protein design?}, url = {http://dx.doi.org/10.1093/bib/2.3.279}, volume = {2}, year = {2001} }

TY - JOUR ID - citeulike:3111897 L3 - citeulike-article-id:3111897 N2 - Evidence from diverse studies, such as protein design experiments and analysis of the emergence of drug resistance in human immunodeficiency virus 1 (HIV-1), indicates that protein function can be diminished or altered by mutations at positions distant from the classic functional' site. Furthermore, results from correlation analysis of the ligand-binding domain of nuclear receptors suggest that mutation events at positions distributed throughout a protein domain may be involved in functional diversification during the evolution of homologous domain families. This review explores potential applications for a protein design procedure based on correlated substitutions. 10.1093/bib/2.3.279 IS - 3 JF - Brief Bioinform EP - 288 TI - Can correlated mutations in protein domain families be used for protein design? VL - 2 SP - 279 KW - correlated_mutations AU - Nagl, Sylvia PY - 2001/01/01/ UR - http://dx.doi.org/10.1093/bib/2.3.279 ER -