1KEF

PDZ1 of SAP90

Summary for 1KEF

• Entry DOI: 10.2210/pdb1kef/pdb
• Descriptor: synapse associated protein-90 (1 entity in total)
• Functional Keywords: beta-sheet, anti-parallel beta-sandwich, glgf loop, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Peripheral membrane protein: P78352
• Total number of polymer chains: 1
• Total formula weight: 10031.26

Authors

Piserchio, A.,Pellegrini, M.,Mehta, S.,Blackman, S.M.,Garcia, E.P.,Marshall, J.,Mierke, D.F. (deposition date: 2001-11-15, release date: 2002-03-06, Last modification date: 2024-05-22)

Primary citation

Piserchio, A.,Pellegrini, M.,Mehta, S.,Blackman, S.M.,Garcia, E.P.,Marshall, J.,Mierke, D.F.
The PDZ1 domain of SAP90. Characterization of structure and binding.
J.Biol.Chem., 277:6967-6973, 2002

PubMed Abstract: The structural features of the PDZ1 domain of the synapse-associated protein SAP90 have been characterized by NMR. A comparison with the structures of the PDZ2 and PDZ3 domains of SAP90 illustrates significant differences, which may account for the unique binding properties of these homologous domains. Within the postsynaptic density, SAP90 functions as a molecular scaffold with a number of the protein-protein interactions mediated through the PDZ1 domain. Here, using fluorescence anisotropy and NMR chemical shift analysis, we have characterized the association of PDZ1 to the C-terminal peptides of the GluR6 subunit of the kainate receptor, voltage-gated K(+) channel Kv1.4, and microtubule-associate protein CRIPT, all of which are known to associate with SAP90. The latter two, which possess the consensus sequence for binding to PDZ domains (T/S-X-V-oh), have low micromolar binding affinities (1.5-15 microm). The C terminus of GluR6, RLPGKETMA-oh, lacking the consensus sequence, binds to PDZ1 of SAP90 with an affinity of 160 microm. The NMR data illustrate that although all three peptides occupy the binding groove capped by the GLGF loop of PDZ1, specific differences are present, consistent with the variation in binding affinities.

PubMed: 11744724
DOI: 10.1074/jbc.M109453200

Experimental method

SOLUTION NMR