Open AccessStructure of the first PDZ domain of human PSD‐93
Author(s) -
Fiorentini Monica,
Nielsen Ann Kallehauge,
Kristensen Ole,
Kastrup Jette S.,
Gajhede Michael
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109043267
Subject(s) - trimer , pdz domain , linker , crystallography , materials science , domain (mathematical analysis) , dimer , chemistry , nuclear magnetic resonance , computer science , physics , biochemistry , mathematics , mathematical analysis , operating system
The crystal structure of the PDZ1 domain of human PSD‐93 has been determined to 2.0 Å resolution. The PDZ1 domain forms a crystallographic trimer that is also predicted to be stable in solution. The main contributions to the stabilization of the trimer seem to arise from interactions involving the PDZ1–PDZ2 linker region at the extreme C‐terminus of PDZ1, implying that the oligomerization that is observed is not of biological significance in full‐length PSD‐93. Comparison of the structures of the binding cleft of PSD‐93 PDZ1 with the previously reported structures of PSD‐93 PDZ2 and PDZ3 as well as of the closely related human PSD‐95 PDZ1 shows that they are very similar in terms of amino‐acid composition. However, the cleft is significantly narrower in PSD‐95. This could be part of the basis of peptide selectivity between PSD‐93 PDZ1 and PSD‐95 PDZ1.