Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations Export

@article{citeulike:887253, abstract = {An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5prime-triphosphate-induced conformational changes that are reflected in binding of adenosine 5prime-triphosphate with positive cooperativity within rings and negative cooperativity between rings. Herein, correlated mutations in chaperonins are analyzed to unravel routes of allosteric communication in GroEL and in its complex with its co-chaperonin GroES. It is shown that analysis of correlated mutations in the chaperonin family can provide information about pathways of allosteric communication within GroEL and between GroEL and GroES. The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system. Proteins 2002;48:611-617. {\copyright} 2002 Wiley-Liss, Inc.}, address = {Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel}, author = {Kass, Itamar and Horovitz, Amnon}, citeulike-article-id = {887253}, citeulike-linkout-0 = {http://dx.doi.org/10.1002/prot.10180}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12211028}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12211028}, citeulike-linkout-3 = {http://www3.interscience.wiley.com/cgi-bin/abstract/96515643/ABSTRACT}, day = {1}, doi = {10.1002/prot.10180}, issn = {1097-0134}, journal = {Proteins: Structure, Function, and Genetics}, keywords = {correlated\_mutations}, month = {September}, number = {4}, pages = {611--617}, posted-at = {2006-10-06 12:06:50}, priority = {2}, title = {Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations}, url = {http://dx.doi.org/10.1002/prot.10180}, volume = {48}, year = {2002} }

TY - JOUR ID - citeulike:887253 L3 - citeulike-article-id:887253 N2 - An interesting example of an allosteric protein is the chaperonin GroEL. It undergoes adenosine 5prime-triphosphate-induced conformational changes that are reflected in binding of adenosine 5prime-triphosphate with positive cooperativity within rings and negative cooperativity between rings. Herein, correlated mutations in chaperonins are analyzed to unravel routes of allosteric communication in GroEL and in its complex with its co-chaperonin GroES. It is shown that analysis of correlated mutations in the chaperonin family can provide information about pathways of allosteric communication within GroEL and between GroEL and GroES. The results are discussed in the context of available structural, genetic, and biochemical data concerning short- and long-range interactions in the GroE system. Proteins 2002;48:611-617. © 2002 Wiley-Liss, Inc. IS - 4 JF - Proteins: Structure, Function, and Genetics SN - 1097-0134 AD - Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel EP - 617 TI - Mapping pathways of allosteric communication in GroEL by analysis of correlated mutations VL - 48 SP - 611 KW - correlated_mutations AU - Kass, Itamar AU - Horovitz, Amnon PY - 2002/09/01/ UR - http://dx.doi.org/10.1002/prot.10180 ER -