6NGG
Crystal structure of human CD160 V58M mutant
Summary for 6NGG
| Entry DOI | 10.2210/pdb6ngg/pdb |
| Descriptor | CD160 antigen (2 entities in total) |
| Functional Keywords | cd160, hvem, btla, gd, immune system |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 26420.18 |
| Authors | Liu, W.,Bonanno, J.,Almo, S.C. (deposition date: 2018-12-21, release date: 2019-07-03, Last modification date: 2024-10-09) |
| Primary citation | Liu, W.,Garrett, S.C.,Fedorov, E.V.,Ramagopal, U.A.,Garforth, S.J.,Bonanno, J.B.,Almo, S.C. Structural Basis of CD160:HVEM Recognition. Structure, 27:1286-1295.e4, 2019 Cited by PubMed Abstract: CD160 is a signaling molecule that interacts with herpes virus entry mediator (HVEM) and contributes to a wide range of immune responses, including T cell inhibition, natural killer cell activation, and mucosal immunity. GPI-anchored and transmembrane isoforms of CD160 share the same ectodomain responsible for HVEM engagement, which leads to bidirectional signaling. Despite the importance of the CD160:HVEM signaling axis and its therapeutic relevance, the structural and mechanistic basis underlying CD160-HVEM engagement has not been described. We report the crystal structures of the human CD160 extracellular domain and its complex with human HVEM. CD160 adopts a unique variation of the immunoglobulin fold and exists as a monomer in solution. The CD160:HVEM assembly exhibits a 1:1 stoichiometry and a binding interface similar to that observed in the BTLA:HVEM complex. Our work reveals the chemical and physical determinants underlying CD160:HVEM recognition and initiation of associated signaling processes. PubMed: 31230945DOI: 10.1016/j.str.2019.05.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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