1dg3: Difference between revisions

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{{STRUCTURE_1dg3|  PDB=1dg3  |  SCENE=  }}  
{{STRUCTURE_1dg3|  PDB=1dg3  |  SCENE=  }}  


'''STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM'''
===STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM===




==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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==About this Structure==
==About this Structure==
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[[Category: Large gtpase family]]
[[Category: Large gtpase family]]
[[Category: Signaling protein]]
[[Category: Signaling protein]]
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Revision as of 23:01, 30 June 2008

File:1dg3.png

Template:STRUCTURE 1dg3

STRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORMSTRUCTURE OF HUMAN GUANYLATE BINDING PROTEIN-1 IN NUCLEOTIDE FREE FORM

Template:ABSTRACT PUBMED 10676968

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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