Publication: MANORAA (Mapping Analogous Nuclei Onto Residue And Affinity) for identifying protein-ligand fragment interaction, pathways and SNPs
Issued Date
2016-01-01
Resource Type
ISSN
13624962
03051048
03051048
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2-s2.0-85020843009
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Mahidol University
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SCOPUS
Bibliographic Citation
Nucleic Acids Research. Vol.44, No.W1 (2016), W514-W521
Suggested Citation
Duangrudee Tanramluk, Lalita Narupiyakul, Ruj Akavipat, Sungsam Gong, Varodom Charoensawan MANORAA (Mapping Analogous Nuclei Onto Residue And Affinity) for identifying protein-ligand fragment interaction, pathways and SNPs. Nucleic Acids Research. Vol.44, No.W1 (2016), W514-W521. doi:10.1093/nar/gkw314 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/43186
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MANORAA (Mapping Analogous Nuclei Onto Residue And Affinity) for identifying protein-ligand fragment interaction, pathways and SNPs
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Abstract
© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. Protein-ligand interaction analysis is an important step of drug design and protein engineering in order to predict the binding affinity and selectivity between ligands to the target proteins. To date, there are more than 100 000 structures available in the Protein Data Bank (PDB), of which ∼30% are protein-ligand (MW below 1000 Da) complexes. We have developed the integrative web server MANORAA (Mapping Analogous Nuclei Onto Residue And Affinity) with the aim of providing a user-friendly web interface to assist structural study and design of protein-ligand interactions. In brief, the server allows the users to input the chemical fragments and present all the unique molecular interactions to the target proteins with available three-dimensional structures in the PDB. The users can also link the ligands of interest to assess possible off-target proteins, human variants and pathway information using our all-in-one integrated tools. Taken together, we envisage that the server will facilitate and improve the study of protein-ligand interactions by allowing observation and comparison of ligand interactions with multiple proteins at the same time.