Molecular dynamics simulation of human LOX-1 provides an explanation for the lack of OxLDL binding to the Trp150Ala mutant |
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| Authors: | Mattia Falconi Silvia Biocca Giuseppe Novelli Alessandro Desideri |
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| Institution: | (1) Department of Biology and Center of Biostatistics and Bioinformatics, University of Rome "Tor Vergata", Via della Ricerca Scientifica, Rome, Italy, 00133;(2) Department of Neuroscience and Center of Biostatistics and Bioinformatics, University of Rome "Tor Vergata", Via di Tor Vergata, 135, Rome, Italy, 00133;(3) Department of Biopathology and Diagnostic Imaging and Center of Biostatistics and Bioinformatics, University of Rome "Tor Vergata", Azienda Ospedaliera Universitaria, Policlinico Tor Vergata Viale Oxford 81, Rome, Italy, 00133 and Fondazione Livio Patrizi, Rome, Italy |
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| Abstract: | Background Dimeric lectin-like oxidized low-density lipoprotein receptor-1 LOX-1 is the target receptor for oxidized low density lipoprotein
in endothelial cells. In vivo assays revealed that in LOX-1 the basic spine arginine residues are important for binding, which is lost upon mutation of
Trp150 with alanine. Molecular dynamics simulations of the wild-type LOX-1 and of the Trp150Ala mutant C-type lectin-like
domains, have been carried out to gain insight into the severe inactivating effect. |
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