Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of a truncated soluble domain of human glioma pathogenesis‐related protein 1
Author(s) -
Bonafé Nathalie,
Zhan Bin,
Bottazzi Maria Elena,
Perez Oriana A.,
Koski Raymond A.,
Asojo Oluwatoyin A.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110035669
Subject(s) - pathogenesis , prostate cancer , glioma , cancer research , cancer , biology , microbiology and biotechnology , chemistry , immunology , genetics
Glioma pathogenesis‐related protein 1 (GLIPR1) is a member of the CAP superfamily that includes proteins from a wide range of eukaryotic organisms. The biological functions of most CAP proteins, including GLIPR1, are unclear. GLIPR1 is up‐regulated in aggressive glioblastomas and contributes to the invasiveness of cultured glioblastoma cells. In contrast, decreased GLIPR1 expression is associated with advanced prostate cancer. Forced GLIPR1 overexpression is pro‐apoptotic in prostate cancer cells and is being tested in clinical trials as an experimental prostate‐cancer therapy. Human GLIPR1 was expressed as a truncated soluble protein (sGLIPR1), purified and crystallized. Useful X‐ray data have been collected to beyond 1.9 Å resolution from a crystal that belonged to the orthorhombic space group P 2 1 2 1 2 with average unit‐cell parameters a = 85.1, b = 79.5, c = 38.9 Å and either a monomer or dimer in the asymmetric unit.