Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 400, Issue 1, Pages 63-70Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.04.053
Keywords
cross-linking; electrostatic interactions; GTPase; hGBP1; self-association
Categories
Funding
- Deutsche Forschungsgemeinschaft [HE 2679/3-1, STU 317/2-1]
- Marie Curie fellowship
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Human guanylate binding protein 1 (hGBP1) belongs to the dynamin superfamily of large GTPases (LGs). In the course of GTP hydrolysis, the protein undergoes structural changes leading to self-assembly of the protein, which is a characteristic property of all family members. For self-assembly, the protein employs two distinct interaction sites, one of which is located within the LG domain of the protein located at the N-terminus, and the second is located in the C-terminal alpha-helical domain. Here, we identify intramolecular contacts between the LG domain and the helical part of hGBP1, which relay nucleotide-dependent structural changes from the N-terminus to the C-terminus and thereby mediate tetramer formation of the protein through a second contact site at the C-terminus. Furthermore, we demonstrate the impact of this intramolecular communication on the enzymatic activity of hGBP1 and on its cellular localization. (C) 2010 Elsevier Ltd. All rights reserved.
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