4GVC
Crystal Structure of T-cell Lymphoma Invasion and Metastasis-1 PDZ in complex with phosphorylated Syndecan1 Peptide
Summary for 4GVC
| Entry DOI | 10.2210/pdb4gvc/pdb |
| Related | 3KZD 3KZE 4GVD |
| Descriptor | T-lymphoma invasion and metastasis-inducing protein 1, Syndecan-1, CHLORIDE ION, ... (6 entities in total) |
| Functional Keywords | phosphorylation, peptide conformational change, new binding pocket, scaffold signaling protein for cell adhesion and cell junction, syndecan1 p1 tyr phosphorylation, sydencan1 n-terminal thr dansylation, signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell junction: Q13009 Membrane; Single-pass type I membrane protein: P18827 |
| Total number of polymer chains | 2 |
| Total formula weight | 11595.70 |
| Authors | Liu, X.,Shepherd, T.R.,Murray, A.M.,Xu, Z.,Fuentes, E.J. (deposition date: 2012-08-30, release date: 2013-03-13, Last modification date: 2024-11-27) |
| Primary citation | Liu, X.,Shepherd, T.R.,Murray, A.M.,Xu, Z.,Fuentes, E.J. The structure of the Tiam1 PDZ domain/ phospho-syndecan1 complex reveals a ligand conformation that modulates protein dynamics. Structure, 21:342-354, 2013 Cited by PubMed Abstract: PDZ (PSD-95/Dlg/ZO-1) domains are protein-protein interaction modules often regulated by ligand phosphorylation. Here, we investigated the specificity, structure, and dynamics of Tiam1 PDZ domain/ligand interactions. We show that the PDZ domain specifically binds syndecan1 (SDC1), phosphorylated SDC1 (pSDC1), and SDC3 but not other syndecan isoforms. The crystal structure of the PDZ/SDC1 complex indicates that syndecan affinity is derived from amino acids beyond the four C-terminal residues. Remarkably, the crystal structure of the PDZ/pSDC1 complex reveals a binding pocket that accommodates the phosphoryl group. Methyl relaxation experiments of PDZ/SCD1 and PDZ/pSDC1 complexes reveal that PDZ-phosphoryl interactions dampen dynamic motions in a distal region of the PDZ domain by decoupling them from the ligand-binding site. Our data are consistent with a selection model by which specificity and phosphorylation regulate PDZ/syndecan interactions and signaling events. Importantly, our relaxation data demonstrate that PDZ/phospho-ligand interactions regulate protein dynamics and their coupling to distal sites. PubMed: 23395182DOI: 10.1016/j.str.2013.01.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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