Reassessing a sparse energetic network within a single protein domain Export

@article{citeulike:2535240, abstract = {10.1073/pnas.0711732105 Understanding the molecular principles that govern allosteric communication is an important goal in protein science. One way allostery could be transmitted is via sparse energetic networks of residues, and one such evolutionary conserved network was identified in the PDZ domain family of proteins by multiple sequence alignment [Lockless SW, Ranganathan R (1999) 286:295\^{a}299]. We have reassessed the energetic coupling of these residues by double mutant cycles together with ligand binding and stability experiments and found that coupling is not a special property of the coevolved network of residues in PDZ domains. The observed coupling for ligand binding is better explained by a distance relationship, where residues close in space are more likely to couple than distal residues. Our study demonstrates that statistical coupling from sequence analysis is not necessarily a reporter of energetic coupling and allostery.}, author = {Chi, Celestine N. and Elfstr\"{o}m, Lisa and Shi, Yao and Sn\"{a}ll, Tord and Engstr\"{o}m, \r{A}ke and Jemth, Per}, citeulike-article-id = {2535240}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0711732105}, citeulike-linkout-1 = {http://www.pnas.org/content/105/12/4679.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/105/12/4679.full.pdf}, citeulike-linkout-3 = {http://www.pnas.org/cgi/content/abstract/105/12/4679}, citeulike-linkout-4 = {http://view.ncbi.nlm.nih.gov/pubmed/18339805}, citeulike-linkout-5 = {http://www.hubmed.org/display.cgi?uids=18339805}, day = {25}, doi = {10.1073/pnas.0711732105}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {allostery}, month = {March}, number = {12}, pages = {4679--4684}, posted-at = {2009-11-12 03:26:14}, priority = {2}, title = {Reassessing a sparse energetic network within a single protein domain}, url = {http://dx.doi.org/10.1073/pnas.0711732105}, volume = {105}, year = {2008} }

TY - JOUR ID - citeulike:2535240 L3 - citeulike-article-id:2535240 N2 - 10.1073/pnas.0711732105 Understanding the molecular principles that govern allosteric communication is an important goal in protein science. One way allostery could be transmitted is via sparse energetic networks of residues, and one such evolutionary conserved network was identified in the PDZ domain family of proteins by multiple sequence alignment [Lockless SW, Ranganathan R (1999) 286:295â299]. We have reassessed the energetic coupling of these residues by double mutant cycles together with ligand binding and stability experiments and found that coupling is not a special property of the coevolved network of residues in PDZ domains. The observed coupling for ligand binding is better explained by a distance relationship, where residues close in space are more likely to couple than distal residues. Our study demonstrates that statistical coupling from sequence analysis is not necessarily a reporter of energetic coupling and allostery. IS - 12 JF - Proceedings of the National Academy of Sciences of the United States of America EP - 4684 TI - Reassessing a sparse energetic network within a single protein domain VL - 105 SP - 4679 KW - allostery AU - Chi, Celestine AU - Elfström, Lisa AU - Shi, Yao AU - Snäll, Tord AU - Engström, Åke AU - Jemth, Per PY - 2008/03/25/ UR - http://dx.doi.org/10.1073/pnas.0711732105 ER -