Expression, purification, crystallization and preliminary X-ray analysis of a truncated soluble domain of human glioma pathogenesis-related protein 1.
Expression, purification, crystallization and preliminary X-ray analysis of a truncated soluble domain of human glioma pathogenesis-related protein 1.
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人胶质瘤发病机制相关蛋白1截短可溶结构域的表达、纯化、结晶和初步X射线分析。
DOI:
10.1107/s1744309110035669
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发表时间:
2010
期刊:
影响因子:
--
通讯作者:
Asojo,OluwatoyinA
中科院分区:
文献类型:
--
作者:
Bonafe,Nathalie;Zhan,Bin;Bottazzi,MariaElena;Perez,OrianaA;Koski,RaymondA;Asojo,OluwatoyinA
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 P21212 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.