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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 1.80Å" /> '''STRUCTURE OF HUMAN ...)
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Revision as of 14:25, 12 November 2007
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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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