Treffer: Ab initio MO studies of interaction mechanisms of Protein Kinase C with cell membranes
Title:
Ab initio MO studies of interaction mechanisms of Protein Kinase C with cell membranes
Source:
Proceedings of the conference on computational physics 2000 New challenges for the new millenium, Gold Coast, Queensland, Australia, December 3-8, 2000Computer physics communications. 142(1-3):140-143
Publisher Information:
Amsterdam: Elsevier Science, 2001.
Publication Year:
2001
Physical Description:
print, 5 ref
Original Material:
INIST-CNRS
Subject Terms:
Computer science, Informatique, Theoretical physics, Physique théorique, Sciences exactes et technologie, Exact sciences and technology, Physique, Physics, Generalites, General, Instruments, appareillage, composants et techniques communs à plusieurs branches de la physique et de l'astronomie, Instruments, apparatus, components and techniques common to several branches of physics and astronomy, Informatique en physique expérimentale, Computers in experimental physics, Modélisation et simulation par ordinateur, Computer modeling and simulation, Enzyme, Enzima, Transferases, Calcul ab initio, Ab initio calculations, Interaction cellulaire, Cell cell interaction, Interacción celular, Kinase, Membrane plasmique, Cell membranes, Modélisation, Modelling, Méthode calcul, Calculation methods, Méthode orbitale moléculaire, Molecular orbital method, Potentiel électrostatique, Electrostatic potential, Potencial electrostático, Protéine, Proteins, PKC, Protein Kinase C
Document Type:
Konferenz
Conference Paper
File Description:
text
Language:
English
Author Affiliations:
Fundamental Research Laboratories NEC Corporation, 34 Miyukigaoka, Tsukuba, 305-8501, Japan
ISSN:
0010-4655
Rights:
Copyright 2002 INIST-CNRS
CC BY 4.0
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
CC BY 4.0
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
Notes:
Metrology
Accession Number:
edscal.13423268
Database:
PASCAL Archive
Weitere Informationen
Protein Kinase C (PKC) is a family of regulatory enzymes. It is considered that binding with phorbol ester which are PKC activators, increases affinity of PKC for the membranes and consequently induces its conformation change. Electrostatic interactions between PKC and the membrane is assumed to be important, and performed ab initio MO calculations of one domain of PKC consisting of 50 amino acids and its complex with the ester is performed to investigate how the electrostatic potential of PKC changes through docking with the substrate. From the calculation, it is shown that the electrostatic potential of PKC near the binding site is dramatically affected through the binding, suggesting attractive interactions with the cell membrane.