1dg3: Difference between revisions
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[[Image:1dg3.gif|left|200px]] | [[Image:1dg3.gif|left|200px]] | ||
'''STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM''' | {{Structure | ||
|PDB= 1dg3 |SIZE=350|CAPTION= <scene name='initialview01'>1dg3</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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}} | |||
'''STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DG3 is a [ | 1DG3 is a [[Single protein]] structure of sequence from [http://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]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10676968 10676968] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:38:00 2008'' | ||
Revision as of 11:38, 20 March 2008
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STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM
OverviewOverview
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.
About this StructureAbout this Structure
1DG3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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