Structure of the first PDZ domain of human PSD-93

Monica Fiorentini; Ann Kallehauge Nielsen; Ole Kristensen; Jette Sandholm Kastrup; Michael Gajhede

doi:10.1107/S1744309109043267

Structure of the first PDZ domain of human PSD-93

Monica Fiorentini, Ann Kallehauge Nielsen, Ole Kristensen, Jette Sandholm Kastrup, Michael Gajhede

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

9 Citations (Scopus)

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.

Original language	English
Journal	Acta Crystallographica. Section F : Structural Biology and Crystallization Communications
Volume	65
Issue number	12
Pages (from-to)	1254-1257
ISSN	1744-3091
DOIs	https://doi.org/10.1107/S1744309109043267
Publication status	Published - 2009

Keywords

Former Faculty of Pharmaceutical Sciences

Access to Document

10.1107/S1744309109043267

Cite this

@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 and Crystallization Communications",

issn = "1744-3091",

publisher = "Wiley",

number = "12",

}

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

SN - 1744-3091

VL - 65

SP - 1254

EP - 1257

JO - Acta Crystallographica. Section F : Structural Biology and Crystallization Communications

JF - Acta Crystallographica. Section F : Structural Biology and Crystallization Communications

IS - 12

ER -