Structure of the first PDZ domain of human PSD-93

Research output: Contribution to journal › Journal article › Research › peer-review

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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

Harvard

Fiorentini, M, Nielsen, AK, Kristensen, O, Kastrup, JS & Gajhede, M 2009, 'Structure of the first PDZ domain of human PSD-93', Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, vol. 65, no. 12, pp. 1254-1257. https://doi.org/10.1107/S1744309109043267

APA

Fiorentini, M., Nielsen, A. K., Kristensen, O., Kastrup, J. S., & Gajhede, M. (2009). Structure of the first PDZ domain of human PSD-93. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications, 65(12), 1254-1257. https://doi.org/10.1107/S1744309109043267

Vancouver

Fiorentini M, Nielsen AK, Kristensen O, Kastrup JS, Gajhede M. Structure of the first PDZ domain of human PSD-93. Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2009;65(12):1254-1257. https://doi.org/10.1107/S1744309109043267

Author

Fiorentini, Monica ; Nielsen, Ann Kallehauge ; Kristensen, Ole ; Kastrup, Jette Sandholm ; Gajhede, Michael. / Structure of the first PDZ domain of human PSD-93. In: Acta Crystallographica. Section F : Structural Biology and Crystallization Communications. 2009 ; Vol. 65, No. 12. pp. 1254-1257.

Bibtex

@article{85c3c460066411df825d000ea68e967b,
title = "Structure of the first PDZ domain of human PSD-93",
abstract = "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.",
keywords = "Former Faculty of Pharmaceutical Sciences",
author = "Monica Fiorentini and Nielsen, {Ann Kallehauge} and Ole Kristensen and Kastrup, {Jette Sandholm} and Michael Gajhede",
year = "2009",
doi = "10.1107/S1744309109043267",
language = "English",
volume = "65",
pages = "1254--1257",
journal = "Acta Crystallographica Section F: Structural Biology Communications",
issn = "2053-230X",
publisher = "Wiley",
number = "12",

}

RIS

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