Rational Protein Design of Paenibacillus barcinonensis Esterase EstA for Kinetic Resolution of Tertiary Alcohols

ChemCatChem ◽  
2010 ◽  
Vol 2 (8) ◽  
pp. 962-967 ◽  
Author(s):  
Arnau Bassegoda ◽  
Giang-Son Nguyen ◽  
Marlen Schmidt ◽  
Robert Kourist ◽  
Pilar Diaz ◽  
...  
Keyword(s):  
Protein Design ◽  
Kinetic Resolution ◽  
Tertiary Alcohols ◽  
Rational Protein Design ◽  
Paenibacillus Barcinonensis

Kinetic Resolution of Tertiary Alcohols

2012 ◽  
pp. 1
Author(s):  
J. Duschmalé ◽  
Y. Arakawa ◽  
H. Wennemers
Keyword(s):  
Kinetic Resolution ◽  
Tertiary Alcohols

scholarly journals Probing active-site residues of pyranose 2-oxidase fromTrametes multicolorby semi-rational protein design

2009 ◽  
Vol 4 (4) ◽  
pp. 535-543 ◽  
Author(s):  
Clara Salaheddin ◽  
Oliver Spadiut ◽  
Roland Ludwig ◽  
Tien-Chye Tan ◽  
Christina Divne ◽  
...  
Keyword(s):  
Protein Design ◽  
Active Site ◽  
Active Site Residues ◽  
Rational Protein Design

scholarly journals Crystallization of interleukin-18 for structure-based inhibitor design

2015 ◽  
Vol 71 (6) ◽  
pp. 710-717
Author(s):  
Brian Krumm ◽  
Xiangzhi Meng ◽  
Yan Xiang ◽  
Junpeng Deng
Keyword(s):  
Protein Design ◽  
Immune Defense ◽  
Interleukin 18 ◽  
Structure Based Drug Design ◽  
Binding Interface ◽  
Naturally Occurring ◽  
Rational Protein Design ◽  
Entropy Reduction ◽  
Low Ionic Strength

Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulatedin vivoby its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.

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