1kef
From Proteopedia
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'''PDZ1 of SAP90''' | '''PDZ1 of SAP90''' | ||
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[[Category: Pellegrini, M.]] | [[Category: Pellegrini, M.]] | ||
[[Category: Piserchio, A.]] | [[Category: Piserchio, A.]] | ||
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| - | [[Category: | + | [[Category: Glgf loop]] |
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Revision as of 19:38, 2 May 2008
PDZ1 of SAP90
Overview
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.
About this Structure
1KEF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The PDZ1 domain of SAP90. Characterization of structure and binding., Piserchio A, Pellegrini M, Mehta S, Blackman SM, Garcia EP, Marshall J, Mierke DF, J Biol Chem. 2002 Mar 1;277(9):6967-73. Epub 2001 Dec 14. PMID:11744724 Page seeded by OCA on Fri May 2 22:38:27 2008
