1dg3
From Proteopedia
(New page: 200px<br /> <applet load="1dg3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dg3, resolution 1.80Å" /> '''STRUCTURE OF HUMAN ...) |
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| - | [[Image:1dg3.gif|left|200px]]<br /> | + | [[Image:1dg3.gif|left|200px]]<br /><applet load="1dg3" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dg3" size=" | + | |
caption="1dg3, resolution 1.80Å" /> | caption="1dg3, resolution 1.80Å" /> | ||
'''STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM'''<br /> | '''STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Interferon-gamma is an immunomodulatory substance that induces the | + | 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 Structure== | ==About this Structure== | ||
| - | 1DG3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1DG3 is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Herrmann, C.]] | [[Category: Herrmann, C.]] | ||
| - | [[Category: Praefcke, G | + | [[Category: Praefcke, G J.K.]] |
[[Category: Prakash, B.]] | [[Category: Prakash, B.]] | ||
[[Category: Renault, L.]] | [[Category: Renault, L.]] | ||
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[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:16:18 2008'' |
Revision as of 10:16, 21 February 2008
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STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM
Overview
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 Structure
1DG3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
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:10676968
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