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10.1007/s10822-007-9148-5 http://scihub22266oqcxt.onion/10.1007/s10822-007-9148-5 C4828239!4828239 !18034309     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\18034309 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Comput+Aided+Mol+Des 2008 ; 22 (9 ): 673-9 Nephropedia Template TP {{tp|p=18034309 |t=2008. Protein-ligand docking with multiple flexible side chains |pdf=|usr=}}{{18034309 }} gab.com Text Protein-ligand docking with multiple flexible side chains JO: J Comput Aided Mol Des http://www.kidney.de/pget.php?&tw=1&pmid=18034309 #FOAvip In this work, we validate and analyze the results of previously published cross docking experiments and classify failed dockings based on the conformational changes observed in the receptors. We show that a majority of failed experiments (i.e. 25 out of 33, involving four different receptors: cAPK, CDK2, Ricin and HIVp) are due to conformational changes in side chains near the active site. For these cases, we identify the side chains to be made flexible during docking calculation by superimposing receptors and analyzing steric overlap between various ligands and receptor side chains. We demonstrate that allowing these side chains to assume rotameric conformations enables the successful cross docking of 19 complexes (ligand all atom RMSD < 2.0 A) using our docking software FLIPDock. The number of side receptor side chains interacting with a ligand can vary according to the ligand's size and shape. Hence, when starting from a complex with a particular ligand one might have to extend the region of potential interacting side chains beyond the ones interacting with the known ligand. We discuss distance-based methods for selecting additional side chains in the neighborhood of the known active site. We show that while using the molecular surface to grow the neighborhood is more efficient than Euclidian-distance selection, the number of side chains selected by these methods often remains too large and additional methods for reducing their count are needed. Despite these difficulties, using geometric constraints obtained from the network of bonded and non-bonded interactions to rank residues and allowing the top ranked side chains to be flexible during docking makes 22 out of 25 complexes successful. Twit Text FOAVip Protein-ligand docking with multiple flexible side chains ????J Comput Aided Mol Des http://www.kidney.de/pget.php?&tw=1&pmid=18034309 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=18034309 #FOAvip English Wikipedia <ref>{{Cite pmid|18034309 }}</ref> Protein-ligand docking with multiple flexible side chains #MMPMID18034309 Zhao Y ; Sanner MF J Comput Aided Mol Des 2008[Sep]; 22 (9 ): 673-9 PMID18034309 show ga In this work, we validate and analyze the results of previously published cross docking experiments and classify failed dockings based on the conformational changes observed in the receptors. We show that a majority of failed experiments (i.e. 25 out of 33, involving four different receptors: cAPK, CDK2, Ricin and HIVp) are due to conformational changes in side chains near the active site. For these cases, we identify the side chains to be made flexible during docking calculation by superimposing receptors and analyzing steric overlap between various ligands and receptor side chains. We demonstrate that allowing these side chains to assume rotameric conformations enables the successful cross docking of 19 complexes (ligand all atom RMSD < 2.0 A) using our docking software FLIPDock. The number of side receptor side chains interacting with a ligand can vary according to the ligand's size and shape. Hence, when starting from a complex with a particular ligand one might have to extend the region of potential interacting side chains beyond the ones interacting with the known ligand. We discuss distance-based methods for selecting additional side chains in the neighborhood of the known active site. We show that while using the molecular surface to grow the neighborhood is more efficient than Euclidian-distance selection, the number of side chains selected by these methods often remains too large and additional methods for reducing their count are needed. Despite these difficulties, using geometric constraints obtained from the network of bonded and non-bonded interactions to rank residues and allowing the top ranked side chains to be flexible during docking makes 22 out of 25 complexes successful. |*Models, Molecular [MESH] |Binding Sites [MESH] |Cyclic AMP-Dependent Protein Kinases/*chemistry/metabolism [MESH] |Cyclin-Dependent Kinase 2/*chemistry/metabolism [MESH] |HIV Protease Inhibitors/chemistry/pharmacology [MESH] |HIV Protease/*chemistry/metabolism [MESH] |Humans [MESH] |Ligands [MESH] |Protein Conformation [MESH]Protein-ligand docking with multiple flexible side chains (epmc).pdf DeepDyve Pubget Overpricing