Home LiteratureArticle Details
PMID: 7964924 Published · ppublish English Journal Article

A shape- and chemistry-based docking method and its use in the design of HIV-1 protease inhibitors.

Journal of computer-aided molecular design ·Vol. 8 ·No. 3 ·1994-06-00 ·Pages 231-42

DesJarlais RL, Dixon JS

Abstract

The program DOCK [1,2] has been used successfully to identify molecules which will bind to a specified receptor [3]. The original method ranks molecules based on their shape complementarity to the receptor site and relies on the chemist to bring the appropriate electrostatic or hydrogen bond properties into the molecular skeletons obtained in the search. This is useful when screening a small database of compounds, where it is not likely that molecules with both the correct shape and electrostatic properties will be found. As large databases are more likely to have redundant molecular shapes with a variety of functionality (e.g., members of a congeneric series), it would be useful to have a method which identifies molecules with both the correct shape and functionality. To this end we have modified the DOCK 1.0 method to target user-specified atom types to selected positions in the receptor site. The target sites can be chosen based on structural evidence, calculation or inspection. Targeted-DOCK improves the ability of the DOCK method to find the crystallographically determined binding mode of a ligand. Additionally, targeted-DOCK searches a database of small molecules at 100-1000 times the rate of DOCK 1.0, allowing more molecules to be screened and more sophisticated scoring schemes to be employed. Targeted-DOCK has been used successfully in the design of a novel non-peptide inhibitor of HIV-1 protease.

MeSH Terms
Binding Sites Drug Design Electrochemistry HIV Protease Inhibitors/chemistry HIV-1/enzymology Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral/chemistry Hydrogen Bonding Molecular Structure N-Acetylneuraminic Acid Sialic Acids/chemistry Software Thermolysin/antagonists & inhibitors,chemistry
Chemicals
HIV Protease Inhibitors Hemagglutinin Glycoproteins, Influenza Virus Hemagglutinins, Viral Sialic Acids Thermolysin N-Acetylneuraminic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
DesJarlais R L
Department of Physical and Structural Chemistry, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406-0939.
Dixon J S
References (26)
26 references, click to expand
  1. Hydroxyethylene isostere inhibitors of human immunodeficiency virus-1 protease: structure-activity analysis using enzyme kinetics, X-ray crystallography, and infected T-cell assays.
    Biochemistry. 1992 Jul 28;31(29):6646-59 PMID: 1637805
  2. Structure-based strategies for drug design and discovery.
    Science. 1992 Aug 21;257(5073):1078-82 PMID: 1509259
  3. Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study.
    Biochemistry. 1989 Oct 17;28(21):8388-96 PMID: 2605190
  4. A symmetric inhibitor binds HIV-1 protease asymmetrically.
    Biochemistry. 1993 Jan 26;32(3):937-47 PMID: 8422397
  5. Automated site-directed drug design using molecular lattices.
    J Mol Graph. 1992 Jun;10(2):66-78, 106 PMID: 1637751
  6. Computer design of bioactive molecules: a method for receptor-based de novo ligand design.
    Proteins. 1991;11(4):314-28 PMID: 1758885
  7. Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease.
    Science. 1990 Aug 3;249(4968):527-33 PMID: 2200122
  8. CLIX: a search algorithm for finding novel ligands capable of binding proteins of known three-dimensional structure.
    Proteins. 1992 Jan;12(1):31-41 PMID: 1313175
  9. Structure of complex of synthetic HIV-1 protease with a substrate-based inhibitor at 2.3 A resolution.
    Science. 1989 Dec 1;246(4934):1149-52 PMID: 2686029
  10. Functionality maps of binding sites: a multiple copy simultaneous search method.
    Proteins. 1991;11(1):29-34 PMID: 1961699
  11. The computer program LUDI: a new method for the de novo design of enzyme inhibitors.
    J Comput Aided Mol Des. 1992 Feb;6(1):61-78 PMID: 1583540
  12. Binding of N-carboxymethyl dipeptide inhibitors to thermolysin determined by X-ray crystallography: a novel class of transition-state analogues for zinc peptidases.
    Biochemistry. 1984 Nov 20;23(24):5724-9 PMID: 6395881
  13. A geometric approach to macromolecule-ligand interactions.
    J Mol Biol. 1982 Oct 25;161(2):269-88 PMID: 7154081
  14. Using shape complementarity as an initial screen in designing ligands for a receptor binding site of known three-dimensional structure.
    J Med Chem. 1988 Apr;31(4):722-9 PMID: 3127588
  15. Areas, volumes, packing and protein structure.
    Annu Rev Biophys Bioeng. 1977;6:151-76 PMID: 326146
  16. X-ray crystallographic structure of a complex between a synthetic protease of human immunodeficiency virus 1 and a substrate-based hydroxyethylamine inhibitor.
    Proc Natl Acad Sci U S A. 1990 Nov;87(22):8805-9 PMID: 2247451
  17. Slow- and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues.
    Biochemistry. 1987 Dec 29;26(26):8542-53 PMID: 3442675
  18. Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bond.
    Science. 1987 Jan 30;235(4788):571-4 PMID: 3810156
  19. The HIV-1 protease as a therapeutic target for AIDS.
    AIDS Res Hum Retroviruses. 1992 Feb;8(2):153-64 PMID: 1540403
  20. Rational design of potent, bioavailable, nonpeptide cyclic ureas as HIV protease inhibitors.
    Science. 1994 Jan 21;263(5145):380-4 PMID: 8278812
  21. The Protein Data Bank: a computer-based archival file for macromolecular structures.
    J Mol Biol. 1977 May 25;112(3):535-42 PMID: 875032
  22. Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
    Biochemistry. 1991 Feb 12;30(6):1600-9 PMID: 1993177
  23. Binding of hydroxamic acid inhibitors to crystalline thermolysin suggests a pentacoordinate zinc intermediate in catalysis.
    Biochemistry. 1981 Nov 24;20(24):6912-20 PMID: 7317361
  24. Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin.
    Eur J Biochem. 1986 Jun 2;157(2):261-8 PMID: 3709536
  25. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules.
    J Med Chem. 1985 Jul;28(7):849-57 PMID: 3892003
  26. Conserved folding in retroviral proteases: crystal structure of a synthetic HIV-1 protease.
    Science. 1989 Aug 11;245(4918):616-21 PMID: 2548279
Article Info
Journal
Journal of computer-aided molecular design
Abbr.
J Comput Aided Mol Des
ISSN
0920-654X
Published
1994-06-00
Pages
231-42
Language
English
Region
Netherlands
NLM ID
8710425
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com