1VJ6
PDZ2 from PTP-BL in complex with the C-terminal ligand from the APC protein
Summary for 1VJ6
| Entry DOI | 10.2210/pdb1vj6/pdb |
| Related | 1gm1 1ozi |
| NMR Information | BMRB: 6060 |
| Descriptor | protein-tyrosine-phosphatase (nonreceptor type 13), Adenomatous polyposis coli protein (2 entities in total) |
| Functional Keywords | pdz, complex, apc, protein-protein interaction, ptp-bl, c-terminus, hydrolase-signaling protein complex, hydrolase/signaling protein |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Cytoplasm, cytoskeleton (By similarity): Q64512 Cell junction, adherens junction (By similarity): Q61315 |
| Total number of polymer chains | 2 |
| Total formula weight | 12194.85 |
| Authors | Walma, T.,Vuister, G.W. (deposition date: 2004-02-03, release date: 2005-11-01, Last modification date: 2024-05-22) |
| Primary citation | Gianni, S.,Walma, T.,Arcovito, A.,Calosci, N.,Bellelli, A.,Engstrom, A.,Travaglini-Allocatelli, C.,Brunori, M.,Jemth, P.,Vuister, G.W. Demonstration of long-range interactions in a PDZ domain by NMR, kinetics, and protein engineering. Structure, 14:1801-1809, 2006 Cited by PubMed Abstract: Understanding the basis of communication within protein domains is a major challenge in structural biology. We present structural and dynamical evidence for allosteric effects in a PDZ domain, PDZ2 from the tyrosine phosphatase PTP-BL, upon binding to a target peptide. The NMR structures of its free and peptide-bound states differ in the orientation of helix alpha2 with respect to the remainder of the molecule, concomitant with a readjustment of the hydrophobic core. Using an ultrafast mixing instrument, we detected a deviation from simple bimolecular kinetics for the association with peptide that is consistent with a rate-limiting conformational change in the protein (k(obs) approximately 7 x 10(3) s(-1)) and an induced-fit model. Furthermore, the binding kinetics of 15 mutants revealed that binding is regulated by long-range interactions, which can be correlated with the structural rearrangements resulting from peptide binding. The homologous protein PSD-95 PDZ3 did not display a similar ligand-induced conformational change. PubMed: 17161370DOI: 10.1016/j.str.2006.10.010 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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