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10.1021/acschembio.7b00056 http://scihub22266oqcxt.onion/10.1021/acschembio.7b00056 C5748325!5748325!28368100     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 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 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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       ACS+Chem+Biol 2017 ; 12 (5): 1204-10 Nephropedia Template TP {{tp|p=28368100|t=2017. Halogen-? Interactions in the Cytochrome P450 Active Site: Structural Insights into Human CYP2B6 Substrate Selectivity |pdf=|usr=}}{{28368100}} gab.com Text Halogen- Interactions in the Cytochrome P450 Active Site: Structural Insights into Human CYP2B6 Substrate Selectivity JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28368100 #FOAvip Numerous cytochrome P450 (CYP)2B6 substrates including drugs and environmental chemicals are halogenated. To assess the role of halogen-? bonds in substrate selectivity and orientation in the active site, structures of four CYP2B6 monoterpenoid complexes were solved by X-ray crystallography. Bornyl bromide exhibited dual orientations in the active site with the predominant orientation revealing a bromine-? bond with the Phe108 side chain. Bornane demonstrated two orientations with equal occupancy; in both the C2-atom that bears the bromine in bornyl bromide was displaced by more than 2.5 Å compared with the latter complex. The bromine in myrtenyl bromide ?-bonded with Phe297 in CYP2B6, whereas the two major orientations in the active site mutant I114V exhibited bromine-? interactions with two additional residues, Phe108 and Phe115. Analysis of existing structures suggests that halogen-? interactions may be unique to the CYP2B enzymes within CYP family 2 but are also important for CYP3A enzymes. Twit Text FOAVip Halogen- Interactions in the Cytochrome P450 Active Site: Structural Insights into Human CYP2B6 Substrate Selectivity ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=28368100 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28368100 #FOAvip English Wikipedia <ref>{{Cite pmid|28368100}}</ref> Halogen-? Interactions in the Cytochrome P450 Active Site: Structural Insights into Human CYP2B6 Substrate Selectivity #MMPMID28368100 Shah MB; Liu J; Zhang Q; Stout CD; Halpert JR ACS Chem Biol 2017[May]; 12 (5): 1204-10 PMID28368100show ga Numerous cytochrome P450 (CYP)2B6 substrates including drugs and environmental chemicals are halogenated. To assess the role of halogen-? bonds in substrate selectivity and orientation in the active site, structures of four CYP2B6 monoterpenoid complexes were solved by X-ray crystallography. Bornyl bromide exhibited dual orientations in the active site with the predominant orientation revealing a bromine-? bond with the Phe108 side chain. Bornane demonstrated two orientations with equal occupancy; in both the C2-atom that bears the bromine in bornyl bromide was displaced by more than 2.5 Å compared with the latter complex. The bromine in myrtenyl bromide ?-bonded with Phe297 in CYP2B6, whereas the two major orientations in the active site mutant I114V exhibited bromine-? interactions with two additional residues, Phe108 and Phe115. Analysis of existing structures suggests that halogen-? interactions may be unique to the CYP2B enzymes within CYP family 2 but are also important for CYP3A enzymes. äHalogen-? Interactions in the Cytochrome P450 Active Site: Structural (epmc).pdf DeepDyve Pubget Overpricing