Back to Search
Start Over
Human cytidine deaminase: understanding the catalytic mechanism
- Source :
- Nucleosides, nucleotidesnucleic acids. 22(5-8)
- Publication Year :
- 2003
-
Abstract
- In the absence of an experimentally elucidated three-dimensional structure of the human CDA, we built an homology model of this enzyme starting from the crystal structure of its E. coli homologous. Furthermore, we docked in the active site alternatively the substrate, the intermediate or the product. By means of molecular dynamics simulations, we determined the topology of the active site, identifying the amino acids involved in the catalytic mechanism, and outlining the central role played by E67.
- Subjects :
- Models, Molecular
Stereochemistry
Protein Conformation
Biochemistry
Catalysis
Protein Structure, Secondary
Molecular dynamics
Cytidine Deaminase
Genetics
Escherichia coli
Humans
Homology modeling
Amino Acid Sequence
Topology (chemistry)
chemistry.chemical_classification
Binding Sites
biology
Escherichia coli Proteins
Active site
Substrate (chemistry)
General Medicine
Cytidine deaminase
Amino acid
Protein Subunits
Enzyme
chemistry
biology.protein
Nucleic acid
Molecular Medicine
Subjects
Details
- ISSN :
- 15257770
- Volume :
- 22
- Issue :
- 5-8
- Database :
- OpenAIRE
- Journal :
- Nucleosides, nucleotidesnucleic acids
- Accession number :
- edsair.doi.dedup.....16e309ccea18b8b2d01056df6a209ace