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

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: 17161370
DOI: 10.1016/j.str.2006.10.010

Experimental method

SOLUTION NMR