Modelling protein docking using shape complementarity, electrostatics and biochemical information

@article{Gabb1997, abstract = {A protein docking study was performed for two classes of biomolecular complexes: six enzyme/inhibitor and four antibody/antigen. Biomolecular complexes for which crystal structures of both the complexed and uncomplexed proteins are available were used for eight of the ten test systems. Our docking experiments consist of a global search of translational and rotational space followed by refinement of the best predictions. Potential complexes are scored on the basis of shape complementarity and favourable electrostatic interactions using Fourier correlation theory. Since proteins undergo conformational changes upon binding, the scoring function must be sufficiently soft to dock unbound structures successfully. Some degree of surface overlap is tolerated to account for side-chain flexibility. Similarly for electrostatics, the interaction of the dispersed point charges of one protein with the Coulombic field of the other is measured rather than precise atomic interactions. We tested our docking protocol using the native rather than the complexed forms of the proteins to address the more scientifically interesting problem of predictive docking. In all but one of our test cases, correctly docked geometries (interface C[alpha] RMS deviation [les] 2 A from the experimental structure) are found during a global search of translational and rotational space in a list that was always less than 250 complexes and often less than 30. Varying degrees of biochemical information are still necessary to remove most of the incorrectly docked complexes.}, author = {Gabb, Henry A. and Jackson, Richard M. and Sternberg, Michael J. }, citeulike-article-id = {410893}, doi = {10.1006/jmbi.1997.1203}, journal = {Journal of Molecular Biology}, keywords = {protein\_docking, structural\_bioinformatics}, month = {September}, number = {1}, pages = {106--120}, posted-at = {2007-09-17 15:40:25}, priority = {2}, title = {Modelling protein docking using shape complementarity, electrostatics and biochemical information}, url = {http://dx.doi.org/10.1006/jmbi.1997.1203}, volume = {272}, year = {1997} }

TY - JOUR ID - Gabb1997 L3 - citeulike-article-id:410893 TI - Modelling protein docking using shape complementarity, electrostatics and biochemical information JF - Journal of Molecular Biology VL - 272 IS - 1 SP - 106 EP - 120 N2 - A protein docking study was performed for two classes of biomolecular complexes: six enzyme/inhibitor and four antibody/antigen. Biomolecular complexes for which crystal structures of both the complexed and uncomplexed proteins are available were used for eight of the ten test systems. Our docking experiments consist of a global search of translational and rotational space followed by refinement of the best predictions. Potential complexes are scored on the basis of shape complementarity and favourable electrostatic interactions using Fourier correlation theory. Since proteins undergo conformational changes upon binding, the scoring function must be sufficiently soft to dock unbound structures successfully. Some degree of surface overlap is tolerated to account for side-chain flexibility. Similarly for electrostatics, the interaction of the dispersed point charges of one protein with the Coulombic field of the other is measured rather than precise atomic interactions. We tested our docking protocol using the native rather than the complexed forms of the proteins to address the more scientifically interesting problem of predictive docking. In all but one of our test cases, correctly docked geometries (interface C[alpha] RMS deviation [les] 2 A from the experimental structure) are found during a global search of translational and rotational space in a list that was always less than 250 complexes and often less than 30. Varying degrees of biochemical information are still necessary to remove most of the incorrectly docked complexes. KW - protein_docking KW - structural_bioinformatics AU - Gabb, Henry AU - Jackson, Richard AU - Sternberg, Michael PY - 1997/09/12/ UR - http://dx.doi.org/10.1006/jmbi.1997.1203 ER -