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Structural basis of mercury- and zinc-conjugated complexes as SARS-CoV 3C-like protease inhibitors
- Source :
- Febs Letters
- Publisher :
- Federation of European Biochemical Societies. Published by Elsevier B.V.
-
Abstract
- Five active metal-conjugated inhibitors (PMA, TDT, EPDTC, JMF1586 and JMF1600) bound with the 3C-like protease of severe acute respiratory syndrome (SARS)-associated coronavirus were analyzed crystallographically. The complex structures reveal two major inhibition modes: Hg(2+)-PMA is coordinated to C(44), M(49) and Y(54) with a square planar geometry at the S3 pocket, whereas each Zn(2+) of the four zinc-inhibitors is tetrahedrally coordinated to the H(41)-C(145) catalytic dyad. For anti-SARS drug design, this Zn(2+)-centered coordination pattern would serve as a starting platform for inhibitor optimization.
- Subjects :
- Models, Molecular
Stereochemistry
TDT, toluene-3,4-dithiolato zinc
medicine.medical_treatment
Biophysics
chemistry.chemical_element
Zinc
Conjugated system
medicine.disease_cause
Biochemistry
Article
BABIM, bis(5-amidino-2-benzimidazolyl) methane
Structure-Activity Relationship
Viral Proteins
Structural Biology
PMA, phenylmercuric acetate
Genetics
medicine
Protease Inhibitors
3c protease
ESI-MS, electrospray ionization mass spectrometry
NMR, nuclear magnetic resonance
Metal ion
Molecular Biology
Coronavirus 3C Proteases
Coronavirus
SARS
Protease
Molecular Structure
Cell Biology
JMF1600, (nitrilotriacetato-N,O) zinc(II) acetate
Cysteine Endopeptidases
Severe acute respiratory syndrome-related coronavirus
chemistry
Protease inhibitor
JMF1586, bis(l-aspartato-N,O) zinc(II) ethanate
EPDTC, N-ethyl-N-phenyldithiocarbamic acid zinc
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 28
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....c1dcb4ebaae08990033a8efd5c00f954
- Full Text :
- https://doi.org/10.1016/j.febslet.2007.10.048