Common physical basis of macromolecule-binding sites in proteins Export

@article{citeulike:3500172, abstract = {Protein-DNA/RNA/protein interactions play critical roles in many biological functions. Previous studies have focused on the different features characterizing the different macromolecule-binding sites and approaches to detect these sites. However, no common unique signature of these sites had been reported. Thus, this work aims to provide a common' principle dictating the location of the different macromolecule-binding sites founded upon fundamental principles of binding thermodynamics. To achieve this aim, a comprehensive set of structurally nonhomologous DNA-, RNA-, obligate protein- and nonobligate protein-binding proteins, both free and bound to their respective macromolecules, was created and a novel strategy for detecting clusters of residues with electrostatic or steric strain given the protein structure was developed. The results show that regardless of the macromolecule type, the binding strength and conformational changes upon binding, macromolecule-binding sites are energetically less stable than nonmacromolecule-binding sites. They also reveal new energetic features distinguishing DNA- from RNA-binding sites and obligate protein- from nonobligate protein-binding sites in both free/bound protein structures. 10.1093/nar/gkn868}, author = {Chen, Yao C. and Lim, Carmay}, citeulike-article-id = {3500172}, citeulike-linkout-0 = {http://dx.doi.org/10.1093/nar/gkn868}, citeulike-linkout-1 = {http://nar.oxfordjournals.org/content/gkn868v1/.abstract}, citeulike-linkout-2 = {http://nar.oxfordjournals.org/content/gkn868v1/.full.pdf}, citeulike-linkout-3 = {http://nar.oxfordjournals.org/cgi/content/abstract/36/22/7078?rss=1}, citeulike-linkout-4 = {http://view.ncbi.nlm.nih.gov/pubmed/18988628}, citeulike-linkout-5 = {http://www.hubmed.org/display.cgi?uids=18988628}, day = {6}, doi = {10.1093/nar/gkn868}, issn = {1362-4962}, journal = {Nucl. Acids Res.}, keywords = {0\_ppi}, month = {November}, pages = {gkn868+}, posted-at = {2008-11-10 07:02:14}, priority = {2}, title = {Common physical basis of macromolecule-binding sites in proteins}, url = {http://dx.doi.org/10.1093/nar/gkn868}, year = {2008} }

TY - JOUR ID - citeulike:3500172 L3 - citeulike-article-id:3500172 N2 - Protein-DNA/RNA/protein interactions play critical roles in many biological functions. Previous studies have focused on the different features characterizing the different macromolecule-binding sites and approaches to detect these sites. However, no common unique signature of these sites had been reported. Thus, this work aims to provide a common' principle dictating the location of the different macromolecule-binding sites founded upon fundamental principles of binding thermodynamics. To achieve this aim, a comprehensive set of structurally nonhomologous DNA-, RNA-, obligate protein- and nonobligate protein-binding proteins, both free and bound to their respective macromolecules, was created and a novel strategy for detecting clusters of residues with electrostatic or steric strain given the protein structure was developed. The results show that regardless of the macromolecule type, the binding strength and conformational changes upon binding, macromolecule-binding sites are energetically less stable than nonmacromolecule-binding sites. They also reveal new energetic features distinguishing DNA- from RNA-binding sites and obligate protein- from nonobligate protein-binding sites in both free/bound protein structures. 10.1093/nar/gkn868 JF - Nucl. Acids Res. SN - 1362-4962 TI - Common physical basis of macromolecule-binding sites in proteins SP - gkn868 KW - 0_ppi AU - Chen, Yao AU - Lim, Carmay PY - 2008/11/06/ UR - http://dx.doi.org/10.1093/nar/gkn868 ER -