PDB: 9 resultsInfo pagesStatus searchChemie searchBIRD

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5QU8	Crystal Structure of symmetric swapped human Nck SH3.1 domain, 0.93A, orthorhombic form IV Descriptor: Cytoplasmic protein NCK1, SODIUM ION Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (0.93 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU3	Crystal Structure of domain swapped human Nck SH3.1, 1.01A, monoclinic Descriptor: Cytoplasmic protein NCK1 Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.02 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QUA	Crystal Structure of swapped human Nck SH3.1 domain, 1.5A, C2221 Descriptor: Cytoplasmic protein NCK1 Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.51 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU1	Crystal Structure of the monomeric human Nck SH3.1 domain, triclinic, 1.08A Descriptor: Cytoplasmic protein NCK1, SULFATE ION Authors: Burger, D, Ruf, A, Benz, J, Schlatter, D, Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.08 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU5	Domain Swap in the first SH3 domain of human Nck1 Descriptor: Cytoplasmic protein NCK1 Authors: Burger, D, Ruf, A, Benz, J, Schlatter, D, Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.11 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU2	Crystal Structure of human Nck SH3.1 in complex with peptide PPPVPNPDY Descriptor: ACE-PRO-PRO-PRO-VAL-PRO-ASN-PRO-ASP-TYR-NH2, Cytoplasmic protein NCK1, SULFATE ION Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.04 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU7	Crystal Structure of swapped human Nck SH3.1 domain, 1.3A, orthorhombic form III Descriptor: Cytoplasmic protein NCK1 Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.27 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU4	Crystal Structure of swapped human Nck SH3.1 domain, 1.05A, orthorhombic form I Descriptor: Cytoplasmic protein NCK1 Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.05 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020
5QU6	Crystal Structure of swapped human Nck SH3.1 domain, 1.8A, triclinic Descriptor: Cytoplasmic protein NCK1 Authors: Rudolph, M.G. Deposit date: 2019-12-13 Release date: 2020-02-12 Last modified: 2024-04-03 Method: X-RAY DIFFRACTION (1.816 Å) Cite: Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. J.Biol.Chem., 295, 2020