Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins

被引:280
作者
Prakash, B [1 ]
Praefcke, GJK [1 ]
Renault, L [1 ]
Wittinghofer, A [1 ]
Herrmann, C [1 ]
机构
[1] Max Planck Inst Mol Physiol, D-44227 Dortmund, Germany
关键词
D O I
10.1038/35000617
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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 (refs 1, 2). These are large GTP-binding proteins of relative molecular mass 67,000 with a high-turnover GTPase activity(3) and an antiviral effect(4). Here we have determined the crystal structure of full-length human GBP1 to 1.8 Angstrom resolution. The amino-terminal 278 residues constitute a modified G domain with a number of insertions compared to the canonical pas 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(5).
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页码:567 / 571
页数:5
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