4FHQ

Crystal Structure of HVEM

Summary for 4FHQ

• Entry DOI: 10.2210/pdb4fhq/pdb
• Related: 1JMA 2AW2
• Descriptor: Tumor necrosis factor receptor superfamily member 14 (2 entities in total)
• Functional Keywords: cysteine rich domain, tnf receptor, structural genomics, psi-biology, protein structure initiative, atoms-to-animals: the immune function network, ifn, tnfrsf, cysteine rich domains, receptor, tnf14, btla, cd160, gd of hsv, membrane, new york structural genomics research consortium (nysgrc), immune system
• Biological source: Homo sapiens (human)
• Cellular location: Membrane ; Single-pass type I membrane protein : Q92956
• Total number of polymer chains: 1
• Total formula weight: 14332.18

Authors

Liu, W.,Zhan, C.,Patskovsky, Y.,Bhosle, R.C.,Nathenson, S.G.,Almo, S.C.,Atoms-to-Animals: The Immune Function Network (IFN),New York Structural Genomics Research Consortium (NYSGRC) (deposition date: 2012-06-06, release date: 2012-07-18, Last modification date: 2024-11-06)

Primary citation

Liu, W.,Vigdorovich, V.,Zhan, C.,Patskovsky, Y.,Bonanno, J.B.,Nathenson, S.G.,Almo, S.C.
Increased Heterologous Protein Expression in Drosophila S2 Cells for Massive Production of Immune Ligands/Receptors and Structural Analysis of Human HVEM.
Mol Biotechnol, 57:914-922, 2015

PubMed Abstract: Many immune ligands and receptors are potential drug targets, which delicately manipulate a wide range of immune responses. We describe here the successful application of an efficient method to dramatically improve the heterologous expression levels in Drosophila Schneider 2 cells, which enables the high-throughput production of several important immune ligands/receptors for raising antibodies, and for the structural and functional analyses. As an example, we purified the protein and characterized the structure of the immune receptor herpesvirus entry mediator (HVEM, TNFRSF14). HVEM is a member of tumor necrosis factor receptor superfamily, which is recognized by herpes simplex virus glycoprotein D (gD) and facilitates viral entry. HVEM participates in a range of interactions with other cell surface molecules, including LIGHT, BTLA, and CD160 to modulate a wide range of immune processes in CD4(+) and CD8(+) T cells, as well as NK cells. Due to the involvement of HVEM in these diverse signaling interactions, crystal structures of HVEM in complex with gD or BTLA have been previously reported. Here, we report the structure of HVEM in the absence of any ligands.

PubMed: 26202493
DOI: 10.1007/s12033-015-9881-2

Experimental method

X-RAY DIFFRACTION (2.251 Å)