Guanylate-binding protein
| Guanylate-binding protein, N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 structure of human guanylate binding protein-1 in nucleotide free form | |||||||||
| Identifiers | |||||||||
| Symbol | GBP | ||||||||
| Pfam | PF02263 | ||||||||
| Pfam clan | CL0023 | ||||||||
| InterPro | IPR015894 | ||||||||
| SCOP | 1dg3 | ||||||||
| SUPERFAMILY | 1dg3 | ||||||||
| |||||||||
| Guanylate-binding protein, C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
structure of human guanylate binding protein-1 in nucleotide free form | |||||||||
| Identifiers | |||||||||
| Symbol | GBP_C | ||||||||
| Pfam | PF02841 | ||||||||
| InterPro | IPR003191 | ||||||||
| SCOP | 1dg3 | ||||||||
| SUPERFAMILY | 1dg3 | ||||||||
| |||||||||
In molecular biology, the guanylate-binding protein family is a family of GTPases that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma (Interferon-inducible GTPase) are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-KD immunity-related GTPases (IRGs), the Mx proteins (MX1, MX2), and the large 65- to 67-kd GTPases. Guanylate-binding proteins (GBP) fall into the last class. In humans, there are seven GBPs (hGBP1-7).[1] Structurally, hGBP1 consists of two domains: a compact globular N-terminal domain harbouring the GTPase function, and an alpha-helical finger-like C-terminal domain.[2] Human GBP1 is secreted from cells without the need of a leader peptide, and has been shown to exhibit antiviral activity against Vesicular stomatitis virus and Encephalomyocarditis virus, as well as being able to regulate the inhibition of proliferation and invasion of endothelial cells in response to IFN-gamma.[3]
References
- ↑ Tripal P, Bauer M, Naschberger E, Mortinger T, Hohenadl C, Cornali E, Thurau M, Sturzl M (January 2007). "Unique features of different members of the human guanylate-binding protein family". J. Interferon Cytokine Res. 27 (1): 44–52. doi:10.1089/jir.2007.0086. PMID 17266443.
- ↑ Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 2000 Feb 3;403(6769):567-71. http://www.nature.com/nature/journal/v403/n6769/full/403567a0.html
- ↑ Naschberger E, Lubeseder-Martellato C, Meyer N, Gessner R, Kremmer E, Gessner A, Sturzl M (September 2006). "Human guanylate binding protein-1 is a secreted GTPase present in increased concentrations in the cerebrospinal fluid of patients with bacterial meningitis". Am. J. Pathol. 169 (3): 1088–99. doi:10.2353/ajpath.2006.060244. PMC 1698817
. PMID 16936281.
This article incorporates text from the public domain Pfam and InterPro IPR003191
This article incorporates text from the public domain Pfam and InterPro IPR015894