Influence of the g- conformation of Ser and Thr on the structure of transmembrane helices. Export

@article{citeulike:5808649, abstract = {In order to study the influence of Ser and Thr on the structure of transmembrane helices we have analyzed a database of helix stretches extracted from crystal structures of membrane proteins and an ensemble of model helices generated by molecular dynamics simulations. Both complementary analyses show that Ser and Thr in the g- conformation induce and/or stabilize a structural distortion in the helix backbone. Using quantum mechanical calculations, we have attributed this effect to the electrostatic repulsion between the side chain Ogamma atom of Ser and Thr and the backbone carbonyl oxygen at position i-3. In order to minimize the repulsive force between these negatively charged oxygens, there is a modest increase of the helix bend angle as well as a local opening of the helix turn preceding Ser/Thr. This small distortion can be amplified through the helix, resulting in a significant displacement of the residues located at the other side of the helix. The crystal structures of aquaporin Z and the beta(2)-adrenergic receptor are used to illustrate these effects. Ser/Thr-induced structural distortions can be implicated in processes as diverse as ligand recognition, protein function and protein folding.}, author = {Deupi, Xavier and Olivella, Mireia and Sanz, Arantxa and D\"{o}lker, Nicole and Campillo, Mercedes and Pardo, Leonardo}, citeulike-article-id = {5808649}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.jsb.2009.09.009}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S1047847709002664}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19766191}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19766191}, day = {17}, doi = {10.1016/j.jsb.2009.09.009}, issn = {1095-8657}, journal = {Journal of structural biology}, keywords = {activation, amber, dynamics, flexibility, hbond, helix, plasticity, ser, structure, theory, tm5}, month = {September}, posted-at = {2009-09-25 14:15:01}, priority = {2}, title = {Influence of the g- conformation of Ser and Thr on the structure of transmembrane helices.}, url = {http://dx.doi.org/10.1016/j.jsb.2009.09.009}, year = {2009} }

TY - JOUR ID - citeulike:5808649 L3 - citeulike-article-id:5808649 N2 - In order to study the influence of Ser and Thr on the structure of transmembrane helices we have analyzed a database of helix stretches extracted from crystal structures of membrane proteins and an ensemble of model helices generated by molecular dynamics simulations. Both complementary analyses show that Ser and Thr in the g- conformation induce and/or stabilize a structural distortion in the helix backbone. Using quantum mechanical calculations, we have attributed this effect to the electrostatic repulsion between the side chain Ogamma atom of Ser and Thr and the backbone carbonyl oxygen at position i-3. In order to minimize the repulsive force between these negatively charged oxygens, there is a modest increase of the helix bend angle as well as a local opening of the helix turn preceding Ser/Thr. This small distortion can be amplified through the helix, resulting in a significant displacement of the residues located at the other side of the helix. The crystal structures of aquaporin Z and the beta(2)-adrenergic receptor are used to illustrate these effects. Ser/Thr-induced structural distortions can be implicated in processes as diverse as ligand recognition, protein function and protein folding. JF - Journal of structural biology SN - 1095-8657 TI - Influence of the g- conformation of Ser and Thr on the structure of transmembrane helices. KW - activation KW - amber KW - dynamics KW - flexibility KW - hbond KW - helix KW - plasticity KW - ser KW - structure KW - theory KW - tm5 AU - Deupi, Xavier AU - Olivella, Mireia AU - Sanz, Arantxa AU - Dölker, Nicole AU - Campillo, Mercedes AU - Pardo, Leonardo PY - 2009/09/17/ UR - http://dx.doi.org/10.1016/j.jsb.2009.09.009 ER -