Inspection of the binding sites of proteinase3 for the design of a highly specific substrate
- Author
- HAJJAR, Eric1 ; KORKMAZ, Brice2 ; GAUTHIER, Francis2 ; BRANDSDAL, Bjøm Olav3 ; WITKO-SARSAT, Véronique4 ; REUTER, Nathalie1
[1] Computational Biology Unit, BCCS, University of Bergen, 5008 Bergen, Norway
[2] INSERM U618, Université François Rabelais, 10 boulevard Tonnellé, 37000 Tours, France
[3] The Norwegian Structural Biology Centre, Faculty of Science, University of Tromsø, 9037 Tromsø, Norway
[4] INSERM U507, Université René Descartes Paris 5, Hôpital Necker, 161 rue de Sèvres, 75015 Paris, France - Source
Journal of medicinal chemistry (Print). 2006, Vol 49, Num 4, pp 1248-1260, 13 p ; ref : 50 ref
- CODEN
- JMCMAR
- ISSN
- 0022-2623
- Scientific domain
- Pharmacology drugs
- Publisher
- American Chemical Society, Washington, DC
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Alignement séquence Energie liaison Etude théorique Interaction hydrophobe Interaction moléculaire Leukocyte elastase Liaison hydrogène Modèle moléculaire Modélisation Myeloblastin Méthode dynamique moléculaire Peptide Propriété thermodynamique Site actif Site fixation Spécificité séquence Substrat Séquence C terminale Enzyme Hydrolases Peptidases Serine endopeptidases
- Keyword (en)
- Sequence alignment Binding energy Theoretical study Hydrophobic interaction Molecular interaction Leukocyte elastase Hydrogen bond Molecular model Modeling Myeloblastin Molecular dynamics method Peptides Thermodynamic properties Active site Binding site Sequence specificity Substrate C terminal-Sequence Enzyme Hydrolases Peptidases Serine endopeptidases
- Keyword (es)
- Alineación secuencia Energía enlace Estudio teórico Interacción molecular Leukocyte elastase Enlace hidrógeno Modelo molecular Modelización Myeloblastin Método dinámico molecular Péptido Propiedad termodinámica Lugar activo Sitio fijación Espicificidad secuencia Substrato Secuencia C terminal Enzima Hydrolases Peptidases Serine endopeptidases
- Classification
- Pascal
- 002 Biological and medical sciences / 002B Medical sciences / 002B02 Pharmacology. Drug treatments / 002B02W Miscellaneous
- Discipline
- General pharmacology
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 17534294
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1021/jm051018t 
https://dx.doi.org/10.1021/jm051018t
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