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| | <StructureSection load='1dg3' size='340' side='right'caption='[[1dg3]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1dg3' size='340' side='right'caption='[[1dg3]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1dg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DG3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1dg3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DG3 FirstGlance]. <br> |
| | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg3 OCA], [https://pdbe.org/1dg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dg3 ProSAT]</span></td></tr> | | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg3 OCA], [https://pdbe.org/1dg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dg3 RCSB], [https://www.ebi.ac.uk/pdbsum/1dg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dg3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GBP1_HUMAN GBP1_HUMAN]] Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.<ref>PMID:22106366</ref>
| + | [https://www.uniprot.org/uniprot/GBP1_HUMAN GBP1_HUMAN] Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.<ref>PMID:22106366</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Herrmann, C]] | + | [[Category: Herrmann C]] |
| - | [[Category: Praefcke, G J.K]] | + | [[Category: Praefcke GJK]] |
| - | [[Category: Prakash, B]] | + | [[Category: Prakash B]] |
| - | [[Category: Renault, L]] | + | [[Category: Renault L]] |
| - | [[Category: Wittinghofer, A]] | + | [[Category: Wittinghofer A]] |
| - | [[Category: Dynamin related]]
| + | |
| - | [[Category: Gbp]]
| + | |
| - | [[Category: Gdp]]
| + | |
| - | [[Category: Gmp]]
| + | |
| - | [[Category: Gtp hydrolysis]]
| + | |
| - | [[Category: Interferon induced]]
| + | |
| - | [[Category: Large gtpase family]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
GBP1_HUMAN Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Interferon-gamma is an immunomodulatory substance that induces the expression of many genes to orchestrate a cellular response and establish the antiviral state of the cell. Among the most abundant antiviral proteins induced by interferon-gamma are guanylate-binding proteins such as GBP1 and GBP2. These are large GTP-binding proteins of relative molecular mass 67,000 with a high-turnover GTPase activity and an antiviral effect. Here we have determined the crystal structure of full-length human GBP1 to 1.8 A resolution. The amino-terminal 278 residues constitute a modified G domain with a number of insertions compared to the canonical Ras structure, and the carboxy-terminal part is an extended helical domain with unique features. From the structure and biochemical experiments reported here, GBP1 appears to belong to the group of large GTP-binding proteins that includes Mx and dynamin, the common property of which is the ability to undergo oligomerization with a high concentration-dependent GTPase activity.
Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins.,Prakash B, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C Nature. 2000 Feb 3;403(6769):567-71. PMID:10676968[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nordmann A, Wixler L, Boergeling Y, Wixler V, Ludwig S. A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. FASEB J. 2012 Mar;26(3):1290-300. doi: 10.1096/fj.11-189886. Epub 2011 Nov 21. PMID:22106366 doi:http://dx.doi.org/10.1096/fj.11-189886
- ↑ 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. PMID:10676968 doi:10.1038/35000617
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