Structure of the first PDZ domain of human PSD-93
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Structure of the first PDZ domain of human PSD-93. / Fiorentini, Monica; Nielsen, Ann Kallehauge; Kristensen, Ole; Kastrup, Jette Sandholm; Gajhede, Michael.
In: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, Vol. 65, No. 12, 2009, p. 1254-1257.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Structure of the first PDZ domain of human PSD-93
AU - Fiorentini, Monica
AU - Nielsen, Ann Kallehauge
AU - Kristensen, Ole
AU - Kastrup, Jette Sandholm
AU - Gajhede, Michael
PY - 2009
Y1 - 2009
N2 - The crystal structure of the PDZ1 domain of human PSD-93 has been determined to 2.0 A 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.
AB - The crystal structure of the PDZ1 domain of human PSD-93 has been determined to 2.0 A 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.
KW - Former Faculty of Pharmaceutical Sciences
U2 - 10.1107/S1744309109043267
DO - 10.1107/S1744309109043267
M3 - Journal article
C2 - 20054121
VL - 65
SP - 1254
EP - 1257
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
SN - 2053-230X
IS - 12
ER -
ID: 17114936