Reassessing a sparse energetic network within a single protein domain

@article{citeulike:2535240, abstract = {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) Science 286:295299]. 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. 10.1073/pnas.0711732105}, author = {Chi, Celestine N. and Elfstrom, Lisa and Shi, Yao and Snall, Tord and Engstrom, Ake and Jemth, Per }, citeulike-article-id = {2535240}, doi = {10.1073/pnas.0711732105}, journal = {Proceedings of the National Academy of Sciences}, keywords = {coevolution, correlated-mutation, domain, sca}, month = {March}, pages = {0711732105+}, posted-at = {2008-03-15 01:26:36}, priority = {2}, title = {Reassessing a sparse energetic network within a single protein domain}, url = {http://dx.doi.org/10.1073/pnas.0711732105}, year = {2008} }

TY - JOUR ID - citeulike:2535240 L3 - citeulike-article-id:2535240 TI - Reassessing a sparse energetic network within a single protein domain JF - Proceedings of the National Academy of Sciences SP - 0711732105 N2 - 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) Science 286:295299]. 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. 10.1073/pnas.0711732105 KW - coevolution KW - correlated-mutation KW - domain KW - sca AU - Chi, Celestine AU - Elfstrom, Lisa AU - Shi, Yao AU - Snall, Tord AU - Engstrom, Ake AU - Jemth, Per PY - 2008/03/13/ UR - http://dx.doi.org/10.1073/pnas.0711732105 ER -