MutationExplorer: a webserver for mutation of proteins and 3D visualization of energetic impacts
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MutationExplorer : a webserver for mutation of proteins and 3D visualization of energetic impacts. / Philipp, Michelle; Moth, Christopher W; Ristic, Nikola; Tiemann, Johanna K S; Seufert, Florian; Panfilova, Aleksandra; Meiler, Jens; Hildebrand, Peter W; Stein, Amelie; Wiegreffe, Daniel; Staritzbichler, René.
In: Nucleic Acids Research, 2024.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - MutationExplorer
T2 - a webserver for mutation of proteins and 3D visualization of energetic impacts
AU - Philipp, Michelle
AU - Moth, Christopher W
AU - Ristic, Nikola
AU - Tiemann, Johanna K S
AU - Seufert, Florian
AU - Panfilova, Aleksandra
AU - Meiler, Jens
AU - Hildebrand, Peter W
AU - Stein, Amelie
AU - Wiegreffe, Daniel
AU - Staritzbichler, René
N1 - © The Author(s) 2024. Published by Oxford University Press on behalf of Nucleic Acids Research.
PY - 2024
Y1 - 2024
N2 - The possible effects of mutations on stability and function of a protein can only be understood in the context of protein 3D structure. The MutationExplorer webserver maps sequence changes onto protein structures and allows users to study variation by inputting sequence changes. As the user enters variants, the 3D model evolves, and estimated changes in energy are highlighted. In addition to a basic per-residue input format, MutationExplorer can also upload an entire replacement sequence. Previously the purview of desktop applications, such an upload can back-mutate PDB structures to wildtype sequence in a single step. Another supported variation source is human single nucelotide polymorphisms (SNPs), genomic coordinates input in VCF format. Structures are flexibly colorable, not only by energetic differences, but also by hydrophobicity, sequence conservation, or other biochemical profiling. Coloring by interface score reveals mutation impacts on binding surfaces. MutationExplorer strives for efficiency in user experience. For example, we have prepared 45 000 PDB depositions for instant retrieval and initial display. All modeling steps are performed by Rosetta. Visualizations leverage MDsrv/Mol*. MutationExplorer is available at: http://proteinformatics.org/mutation_explorer/.
AB - The possible effects of mutations on stability and function of a protein can only be understood in the context of protein 3D structure. The MutationExplorer webserver maps sequence changes onto protein structures and allows users to study variation by inputting sequence changes. As the user enters variants, the 3D model evolves, and estimated changes in energy are highlighted. In addition to a basic per-residue input format, MutationExplorer can also upload an entire replacement sequence. Previously the purview of desktop applications, such an upload can back-mutate PDB structures to wildtype sequence in a single step. Another supported variation source is human single nucelotide polymorphisms (SNPs), genomic coordinates input in VCF format. Structures are flexibly colorable, not only by energetic differences, but also by hydrophobicity, sequence conservation, or other biochemical profiling. Coloring by interface score reveals mutation impacts on binding surfaces. MutationExplorer strives for efficiency in user experience. For example, we have prepared 45 000 PDB depositions for instant retrieval and initial display. All modeling steps are performed by Rosetta. Visualizations leverage MDsrv/Mol*. MutationExplorer is available at: http://proteinformatics.org/mutation_explorer/.
U2 - 10.1093/nar/gkae301
DO - 10.1093/nar/gkae301
M3 - Journal article
C2 - 38647044
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 0305-1048
M1 - gkae301
ER -
ID: 390591734