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Author(s) -
Chen Jiangang,
Deng Qiaolin,
Wang Renxiao,
Houk Kendall N.,
Hilvert Donald
Publication year - 2000
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20001117)1:4<207::aid-cbic207>3.0.co;2-3
Subject(s) - active site , chemistry , stacking , molecular dynamics , hydrogen bond , complementarity (molecular biology) , docking (animal) , transition state , catalysis , complementarity determining region , ligand (biochemistry) , stereochemistry , chemical physics , computational chemistry , crystallography , molecule , receptor , organic chemistry , biology , medicine , biochemistry , nursing , gene , peptide sequence , genetics
The cover picture shows the active site of the catalytic antibody 1E9, which promotes the bimolecular Diels–Alder reaction between tetrachlorothiophene dioxide and N ‐ethylmaleimide. Docking and molecular dynamics simulations of the reactant complex (green) and the endo ‐transition state (yellow) bound at the antibody active site illustrate the excellent shape complementarity between ligand and protein. Residues Trp H50 and Asn H35, which interact with the dienophile through π‐stacking and hydrogen bonding, respectively, are seen at the bottom of the active site beneath the transparent protein surface. More about shape complementarity, binding site dynamics, and transition state stabilization can be found in the theoretical study by K. N. Houk, D. Hilvert et al. on p. 255 ff. (The cover image was produced by Kinya Hotta.)