Computational design of affinity and specificity at protein–protein interfaces Export

@article{citeulike:5390366, abstract = {The computer-based design of protein-protein interactions is a rigorous test of our understanding of molecular recognition and an attractive approach for creating novel tools for cell and molecular research. Considerable attention has been placed on redesigning the affinity and specificity of naturally occurring interactions. Several studies have shown that reducing the desolvation costs for binding while preserving shape complimentarity and hydrogen bonding is an effective strategy for improving binding affinities. In favorable cases specificity has been designed by focusing only on interactions with the target protein, while in cases with closely related off-target proteins it has been necessary to explicitly disfavor unwanted binding partners. The rational design of protein-protein interactions from scratch is still an unsolved problem, but recent developments in flexible backbone design and energy functions hold promise for the future.}, author = {Karanicolas, John and Kuhlman, Brian}, citeulike-article-id = {5390366}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.sbi.2009.07.005}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0959440X09000992}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19646858}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19646858}, day = {29}, doi = {10.1016/j.sbi.2009.07.005}, issn = {0959440X}, journal = {Current Opinion in Structural Biology}, keywords = {protein\_protein, review}, month = {August}, number = {4}, pages = {458--463}, posted-at = {2009-08-06 23:48:47}, priority = {2}, title = {Computational design of affinity and specificity at protein–protein interfaces}, url = {http://dx.doi.org/10.1016/j.sbi.2009.07.005}, volume = {19}, year = {2009} }

TY - JOUR ID - citeulike:5390366 L3 - citeulike-article-id:5390366 N2 - The computer-based design of protein-protein interactions is a rigorous test of our understanding of molecular recognition and an attractive approach for creating novel tools for cell and molecular research. Considerable attention has been placed on redesigning the affinity and specificity of naturally occurring interactions. Several studies have shown that reducing the desolvation costs for binding while preserving shape complimentarity and hydrogen bonding is an effective strategy for improving binding affinities. In favorable cases specificity has been designed by focusing only on interactions with the target protein, while in cases with closely related off-target proteins it has been necessary to explicitly disfavor unwanted binding partners. The rational design of protein-protein interactions from scratch is still an unsolved problem, but recent developments in flexible backbone design and energy functions hold promise for the future. IS - 4 JF - Current Opinion in Structural Biology SN - 0959440X EP - 463 TI - Computational design of affinity and specificity at protein–protein interfaces VL - 19 SP - 458 KW - protein_protein KW - review AU - Karanicolas, John AU - Kuhlman, Brian PY - 2009/08/29/ UR - http://dx.doi.org/10.1016/j.sbi.2009.07.005 ER -