Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding
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Tőke, O.; Koprivanacz, K.; Radnai, L.; Merő, B.; Juhász, T.; Liliom, K.; Buday, L. Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding. Cells 2021, 10, 173. https://doi.org/10.3390/cells10010173
Tőke O, Koprivanacz K, Radnai L, Merő B, Juhász T, Liliom K, Buday L. Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding. Cells. 2021; 10(1):173. https://doi.org/10.3390/cells10010173
Chicago/Turabian StyleTőke, Orsolya; Koprivanacz, Kitti; Radnai, László; Merő, Balázs; Juhász, Tünde; Liliom, Károly; Buday, László. 2021. "Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding" Cells 10, no. 1: 173. https://doi.org/10.3390/cells10010173