3Q2R: crystal structure of sGLIPR1 soaked with zinc chloride

Acta Crystallogr. D Biol. Crystallogr. (2011) 67 p.847-855
Human glioma pathogenesis-related protein 1 (GLIPR1) is a membrane protein that is highly upregulated in brain cancers but is barely detectable in normal brain tissue. GLIPR1 is composed of a signal peptide that directs its secretion, a conserved cysteine-rich CAP (cysteine-rich secretory proteins, antigen 5 and pathogenesis-related 1 proteins) domain and a transmembrane domain. GLIPR1 is currently being investigated as a candidate for prostate cancer gene therapy and for glioblastoma targeted therapy. Crystal structures of a truncated soluble domain of the human GLIPR1 protein (sGLIPR1) solved by molecular replacement using a truncated polyalanine search model of the CAP domain of stecrisp, a snake-venom cysteine-rich secretory protein (CRISP), are presented. The correct molecular-replacement solution could only be obtained by removing all loops from the search model. The native structure was refined to 1.85 A resolution and that of a Zn2+ complex was refined to 2.2 A resolution. The latter structure revealed that the putative binding cavity coordinates Zn2+ similarly to snake-venom CRISPs, which are involved in Zn2+-dependent mechanisms of inflammatory modulation. Both sGLIPR1 structures have extensive flexible loop/turn regions and unique charge distributions that were not observed in any of the previously reported CAP protein structures. A model is also proposed for the structure of full-length membrane-bound GLIPR1.
PDB ID: 3Q2RDownload
MMDB ID: 94030
PDB Deposition Date: 2010/12/20
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 3Q2R: monomeric; determined by author
Molecular Components in 3Q2R
Label Count Molecule
Protein (1 molecule)
Glioma Pathogenesis-related Protein 1(Gene symbol: GLIPR1)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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