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Investigating the ATP-binding pocket of CX3CL1-binding protein 2 using in silico approach
Open accessPublished version of a preprint
Abstract
Abstract Plasmodium falciparum (Pf) causes the most fatal form of malaria owing to its ability to cytoadhere in the microvasculature of various organs in the body. In addition to the Pf erythrocyte membrane protein 1 (PfEMP1) family that binds diverse host receptors, CX3CL1 binding proteins 1 and 2 (CBP1 and 2) also bind the endothelial chemokine ‘CX3CL1’ to effect cytoadhesion of parasite infected erthrocytes. CBP2 is a multifaceted protein that binds nucleic acids, Pf skeleton binding protein (PfSBP1) and ATP. ATP binding to the cytoplasmic domain of CBP2 (cCBP2) induces structural changes in the protein, and hints at its role in cell signaling. In this study, we have attempted to identify the ATP binding pocket of CBP2 using an in silico approach. We have also delineated the type of interactions and amino acid residues that are likely to bind ATP. As CX3CL1 binding proteins are central to parasite biology, the obtained information is likely to form the basis for inhibitor and drug design against this molecule.
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Research works printed but not linked: 2
- Honorato Rodrigo V, Koukos Panagiotis I, Jiménez-García Brian, Tsaregorodtsev Andrei, Verlato Marco, Giachetti Andrea, Rosato Antonio, Bonvin Alexandre MJJ (2021) Structural biology in the clouds: the WeNMR-EOSC ecosystem. Front Mol Biosci 8:729513. https://doi.org/10.3389/fmolb.2021.729513/full · DOI
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Metadata
- Authors
- Kumari, R., Kaur, S., Hora, R., & Mishra, P. C.
- Affiliations
- Guru Nanak Dev University (IN)
- Corresponding author
- Mishra, Prakash Chandra
- Venue
- Journal of Proteins and Proteomics
- Published
- 2024-03-26
- Volume
- 15
- Issue
- 2
- Pages
- 209-214
- ISSN
- 0975-8151 (ISSN-L)
- 2524-4663
- OpenAlex
- W4393181328
- Cited by
- 0
- References
- 36
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- green
- dx.doi.org
- Licence
- Locations
- Journal of Proteins and Proteomics (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Research Square (acceptedVersion, cc-by)
- Funders
- Department of Biotechnology, Ministry of Science and Technology, India
- Department of Science and Technology, Ministry of Science and Technology, India
- Topics
- Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Malaria Research and Control
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Drug Discovery › Computational Drug Discovery Methods
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- ATP binding site, Plasmodium falciparum, cytoadhesion, PfEMP1, fractalkine, chemokine binding, ATP binding, protein structure, therapeutic target, inhibitor design
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- Kumari, R., Kaur, S., Hora, R., & Mishra, P. C. (2024). Investigating the ATP-binding pocket of CX3CL1-binding protein 2 using in silico approach. Journal of Proteins and Proteomics. https://doi.org/10.1007/s42485-024-00133-z
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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