Summary: Guanylate-binding protein, C-terminal domain
This is the Wikipedia entry entitled "Guanylate-binding protein". More...
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Guanylate-binding protein Edit Wikipedia article
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|Guanylate-binding protein, N-terminal domain|
structure of human guanylate binding protein-1 in nucleotide free form
|Guanylate-binding protein, C-terminal domain|
structure of human guanylate binding protein-1 in nucleotide free form
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). 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. 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.
- 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.
Guanylate-binding protein, C-terminal domain Provide feedback
Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C; , Nature 2000;403:567-571.: Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. PUBMED:10676968 EPMC:10676968
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003191
Guanylate-binding protein is a GTPase that is induced by interferon (IFN)-gamma. GTPases induced by IFN-gamma are key to the protective immunity against microbial and viral pathogens. These GTPases are classified into three groups: the small 47-kd GTPases, the Mx proteins, 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) [PUBMED:17266443]. Structurally, hGBP1 consists of two domains: a compact globular N-terminal domain harbouring the GTPase function (INTERPRO), and an alpha-helical finger-like C-terminal domain. 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 [PUBMED:16936281].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||GTP binding (GO:0005525)|
|GTPase activity (GO:0003924)|
- the number of sequences which exhibit this architecture
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This example describes an architecture with one
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EGFdomains, and finally a single
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Curation and family details
|Seed source:||Pfam-B_4308 (release 5.2)|
|Author:||Bateman A, Mian N, Griffiths-Jones SR|
|Number in seed:||23|
|Number in full:||678|
|Average length of the domain:||220.50 aa|
|Average identity of full alignment:||29 %|
|Average coverage of the sequence by the domain:||37.66 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the GBP_C domain has been found. There are 9 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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