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3FC0

1.8 A crystal structure of murine GITR ligand dimer expressed in Drosophila melanogaster S2 cells

Summary for 3FC0
Entry DOI10.2210/pdb3fc0/pdb
Related2QDN
DescriptorGITR ligand, ACETATE ION (3 entities in total)
Functional Keywordsgitrl; glucocorticoid-induced tnf receptor ligand, receptor, protein binding
Biological sourceMus musculus (mouse)
Cellular locationCell membrane ; Single-pass type II membrane protein : Q7TS55
Total number of polymer chains2
Total formula weight31863.64
Authors
Chattopadhyay, K.,Ramagopal, U.A.,Nathenson, S.G.,Almo, S.C. (deposition date: 2008-11-20, release date: 2008-12-30, Last modification date: 2024-10-16)
Primary citationChattopadhyay, K.,Ramagopal, U.A.,Nathenson, S.G.,Almo, S.C.
1.8 A structure of murine GITR ligand dimer expressed in Drosophila melanogaster S2 cells.
Acta Crystallogr.,Sect.D, 65:434-439, 2009
Cited by
PubMed Abstract: Glucocorticoid-induced TNF receptor ligand (GITRL), a prominent member of the TNF superfamily, activates its receptor on both effector and regulatory T cells to generate critical costimulatory signals that have been implicated in a wide range of T-cell immune functions. The crystal structures of murine and human orthologs of GITRL recombinantly expressed in Escherichia coli have previously been determined. In contrast to all classical TNF structures, including the human GITRL structure, murine GITRL demonstrated a unique ;strand-exchanged' dimeric organization. Such a novel assembly behavior indicated a dramatic impact on receptor activation as well as on the signaling mechanism associated with the murine GITRL costimulatory system. In this present work, the 1.8 A resolution crystal structure of murine GITRL expressed in Drosophila melanogaster S2 cells is reported. The eukaryotic protein-expression system allows transport of the recombinant protein into the extracellular culture medium, thus maximizing the possibility of obtaining correctly folded material devoid of any folding/assembly artifacts that are often suspected with E. coli-expressed proteins. The S2 cell-expressed murine GITRL adopts an identical ;strand-exchanged' dimeric structure to that observed for the E. coli-expressed protein, thus conclusively demonstrating the novel quaternary structure assembly behavior of murine GITRL.
PubMed: 19390148
DOI: 10.1107/S0907444909005721
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.76 Å)
Structure validation

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数据于2025-10-08公开中

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