Antagonism of the TXA2 receptor by seratrodast: A structural approach

Bioorganic and Medicinal Chemistry Letters

Volumn 9, Issue 19, 1999, Pages 2867-2870

  Wouters, Johan ^a   Durant, François ^a   Masereel, Bernard ^a  

^a UNIVERSITY OF NAMUR   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

DOCKING PROTEIN; SERATRODAST; THROMBOXANE A2 RECEPTOR; THROMBOXANE A2 RECEPTOR BLOCKING AGENT;

ARTICLE; BIOLOGICAL MODEL; CRYSTAL STRUCTURE; DRUG ANTAGONISM; DRUG BINDING; DRUG DESIGN; DRUG SYNTHESIS; HUMAN; HUMAN CELL; LIGAND BINDING; RECEPTOR BINDING; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

ANIMALS; BENZOQUINONES; CRYSTALLOGRAPHY, X-RAY; DRUG DESIGN; GUINEA PIGS; HEPTANOIC ACIDS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; PROSTAGLANDIN ANTAGONISTS; RECEPTORS, THROMBOXANE; SULFONAMIDES;

EID: 0033523648     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-894X(99)00490-4     Document Type: Article

References (8)

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2. 2. Masereel, B. et al. J. Pharm. Pharmacol. 1999, 51, 695-701.
3. 2 using the program Shelxl97 (Sheldrick, G. Univ Goettingen, Germany). Data have been corrected for absorption effects. The hydrogen of the terminal carboxylic acid has not been assigned. Lists of atomic coordinates, displacement parameters, and complete geometry have been deposited with the IUCr.
4. 4. Hirata, M.; et al. Nature 1991, 349, 617-620.
5. 5. Yamamoto, Y.; Kamiya, K.; Terao, S. J. Med. Chem. 1993, 36, 820-825.
6. 5 The rest of the antagonist was adjusted in the binding site of the receptor in order to minimize unfavorable steric contacts. The manual docking was followed by energy minimization (steepest descent and conjugated gradient procedure). All residues further than 6Å from the ligand were fixed. The solvent effect was approached by using a distance dependent dielectric constant (l*r). The complexes (receptor plus either the R or the S isomer) were energy minimized until the energy gradient dropped below 0.01 kcal/mol.
7. 7. Soyka, R. et al. J.Med. Chem. 1999, 42, 1235-1249.
8. 8. Masereel, B. et al. Eur. J. Med. Chem. 1995 , 30, 343-351.