Insight into the Inhibition of Human Choline Kinase: Homology Modeling and Molecular Dynamics Simulations
A homology model of human choline kinase (CK‐α) based on the X‐ray crystallographic structure of C. elegans choline kinase (CKA‐2) is presented. Molecular dynamics simulations performed on CK‐α confirm the quality of the model, and also support the putative ATP and choline binding sites. A good corr...
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| Published in | ChemMedChem Vol. 1; no. 11; pp. 1216 - 1228 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English German |
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Weinheim
WILEY-VCH Verlag
13.11.2006
WILEY‐VCH Verlag |
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| Abstract | A homology model of human choline kinase (CK‐α) based on the X‐ray crystallographic structure of C. elegans choline kinase (CKA‐2) is presented. Molecular dynamics simulations performed on CK‐α confirm the quality of the model, and also support the putative ATP and choline binding sites. A good correlation between the MD results and reported CKA‐2 mutagenesis assays has been found for the main residues involved in catalytic activity. Preliminary docking studies performed on the CK‐α model indicate that inhibitors can bind to the binding sites of both substrates (ATP and choline). A possible reason for inhibition of choline kinase by Ca2+ ion is also proposed.
A homology model of human choline kinase (CK‐α) is presented. Molecular dynamics simulations confirm its quality and support the putative ATP (red) and choline (green) binding sites. MD results are concordant with reported C. elegans choline kinase (CKA‐2) mutagenesis. Preliminary docking studies indicate that inhibitors (white) can bind into both binding sites. |
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| AbstractList | A homology model of human choline kinase (CK-alpha) based on the X-ray crystallographic structure of C. elegans choline kinase (CKA-2) is presented. Molecular dynamics simulations performed on CK-alpha confirm the quality of the model, and also support the putative ATP and choline binding sites. A good correlation between the MD results and reported CKA-2 mutagenesis assays has been found for the main residues involved in catalytic activity. Preliminary docking studies performed on the CK-alpha model indicate that inhibitors can bind to the binding sites of both substrates (ATP and choline). A possible reason for inhibition of choline kinase by Ca(2+) ion is also proposed. A homology model of human choline kinase (CK-) based on the X-ray crystallographic structure of C. elegans choline kinase (CKA-2) is presented. Molecular dynamics simulations performed on CK- confirm the quality of the model, and also support the putative ATP and choline binding sites. A good correlation between the MD results and reported CKA-2 mutagenesis assays has been found for the main residues involved in catalytic activity. Preliminary docking studies performed on the CK- model indicate that inhibitors can bind to the binding sites of both substrates (ATP and choline). A possible reason for inhibition of choline kinase by Ca2+ ion is also proposed. Abstract A homology model of human choline kinase (CK‐α) based on the X‐ray crystallographic structure of C. elegans choline kinase (CKA‐2) is presented. Molecular dynamics simulations performed on CK‐α confirm the quality of the model, and also support the putative ATP and choline binding sites. A good correlation between the MD results and reported CKA‐2 mutagenesis assays has been found for the main residues involved in catalytic activity. Preliminary docking studies performed on the CK‐α model indicate that inhibitors can bind to the binding sites of both substrates (ATP and choline). A possible reason for inhibition of choline kinase by Ca 2+ ion is also proposed. A homology model of human choline kinase (CK‐α) based on the X‐ray crystallographic structure of C. elegans choline kinase (CKA‐2) is presented. Molecular dynamics simulations performed on CK‐α confirm the quality of the model, and also support the putative ATP and choline binding sites. A good correlation between the MD results and reported CKA‐2 mutagenesis assays has been found for the main residues involved in catalytic activity. Preliminary docking studies performed on the CK‐α model indicate that inhibitors can bind to the binding sites of both substrates (ATP and choline). A possible reason for inhibition of choline kinase by Ca2+ ion is also proposed. A homology model of human choline kinase (CK‐α) is presented. Molecular dynamics simulations confirm its quality and support the putative ATP (red) and choline (green) binding sites. MD results are concordant with reported C. elegans choline kinase (CKA‐2) mutagenesis. Preliminary docking studies indicate that inhibitors (white) can bind into both binding sites. |
| Author | Espinosa, Antonio Milanese, Lara Gallo, Miguel A. Campos, Joaquín M. Entrena, Antonio |
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| Snippet | A homology model of human choline kinase (CK‐α) based on the X‐ray crystallographic structure of C. elegans choline kinase (CKA‐2) is presented. Molecular... A homology model of human choline kinase (CK-alpha) based on the X-ray crystallographic structure of C. elegans choline kinase (CKA-2) is presented. Molecular... Abstract A homology model of human choline kinase (CK‐α) based on the X‐ray crystallographic structure of C. elegans choline kinase (CKA‐2) is presented.... A homology model of human choline kinase (CK-) based on the X-ray crystallographic structure of C. elegans choline kinase (CKA-2) is presented. Molecular... |
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| SubjectTerms | Amino Acid Sequence Animals Caenorhabditis elegans - enzymology choline kinase Choline Kinase - antagonists & inhibitors Choline Kinase - chemistry Crystallography, X-Ray homology modeling Humans inhibition Models, Molecular molecular dynamics Molecular Sequence Data Sequence Homology, Amino Acid |
| Title | Insight into the Inhibition of Human Choline Kinase: Homology Modeling and Molecular Dynamics Simulations |
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