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1dg3

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(New page: 200px<br /> <applet load="1dg3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dg3, resolution 1.80&Aring;" /> '''STRUCTURE OF HUMAN ...)
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caption="1dg3, resolution 1.80&Aring;" />
'''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==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DG3 OCA].
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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.]]
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[[Category: Praefcke, G.J.K.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:32:02 2007''
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''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


1dg3, resolution 1.80Å

Drag the structure with the mouse to rotate

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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