Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein

Imran Dar; Christophe Bonny; Jan Torleif Pedersen; Michael Gajhede; Ole Kristensen

doi:10.1107/S0907444903020304

Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein

Imran Dar, Christophe Bonny, Jan Torleif Pedersen, Michael Gajhede, Ole Kristensen

2 Citations (Scopus)

Abstract

IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.

Original language	English
Journal	Acta Crystallographica. Section D: Biological Crystallography
Volume	59
Issue number	Pt 12
Pages (from-to)	2300-2
Number of pages	3
ISSN	0907-4449
DOIs	https://doi.org/10.1107/S0907444903020304
Publication status	Published - 2003

Keywords

Crystallization
Crystallography, X-Ray
Nuclear Proteins
Recombinant Fusion Proteins
Selenomethionine
Trans-Activators
src Homology Domains

Access to Document

10.1107/S0907444903020304

Cite this

@article{493172ca39824e5f922a9e4894c0ecbb,

title = "Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein",

abstract = "IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.",

keywords = "Crystallization, Crystallography, X-Ray, Nuclear Proteins, Recombinant Fusion Proteins, Selenomethionine, Trans-Activators, src Homology Domains",

author = "Imran Dar and Christophe Bonny and Pedersen, {Jan Torleif} and Michael Gajhede and Ole Kristensen",

year = "2003",

doi = "10.1107/S0907444903020304",

language = "English",

volume = "59",

pages = "2300--2",

journal = "Acta Crystallographica Section D: Structural Biology",

issn = "2059-7983",

publisher = "International Union of Crystallography",

number = "Pt 12",

}

TY - JOUR

T1 - Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein

AU - Dar, Imran

AU - Bonny, Christophe

AU - Pedersen, Jan Torleif

AU - Gajhede, Michael

AU - Kristensen, Ole

PY - 2003

Y1 - 2003

N2 - IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.

AB - IB1 is a mammalian scaffold protein that interacts with components of the c-Jun N-terminal kinase (JNK) signal-transduction pathway mainly via its protein-protein interaction domains. Crystallization of the key Src homology 3 (SH3) domain of IB1 has been achieved. Crystallization experiments with unmodified protein and deliberately oxidized protein have led to different crystal forms. X-ray data have been collected to 3.0 A resolution from a crystal form with rectangular prism morphology. These crystals are orthorhombic (P2(1)2(1)2(1)), with unit-cell parameters a = 45.9, b = 57.0, c = 145.5 A. These are the first crystallographic data on a scaffold molecule such as IB1 to be reported.

KW - Crystallization

KW - Crystallography, X-Ray

KW - Nuclear Proteins

KW - Recombinant Fusion Proteins

KW - Selenomethionine

KW - Trans-Activators

KW - src Homology Domains

U2 - 10.1107/S0907444903020304

DO - 10.1107/S0907444903020304

M3 - Journal article

C2 - 14646101

SN - 2059-7983

VL - 59

SP - 2300

EP - 2302

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

IS - Pt 12

ER -

Crystallization and preliminary crystallographic characterization of an SH3 domain from the IB1 scaffold protein

Abstract

Keywords

Access to Document

Fingerprint

Cite this