| First Author | Vigdorovich V | Year | 2013 |
| Journal | Structure | Volume | 21 |
| Issue | 5 | Pages | 707-17 |
| PubMed ID | 23583036 | Mgi Jnum | J:245240 |
| Mgi Id | MGI:5914141 | Doi | 10.1016/j.str.2013.03.003 |
| Citation | Vigdorovich V, et al. (2013) Structure and T cell inhibition properties of B7 family member, B7-H3. Structure 21(5):707-17 |
| abstractText | T cell activity is controlled by a combination of antigen-dependent signaling through the T cell receptor and a set of auxiliary signals delivered through antigen-independent interactions, including the recognition of the B7 family of ligands. B7-H3 is a recently identified B7 family member that is strongly overexpressed in a range of cancers and correlates with poor prognosis. We report the crystal structure of murine B7-H3 at a 3 A resolution, which provides a model for the organization of the IgV and IgC domains within the ectodomain. We demonstrate that B7-H3 inhibits T cell proliferation and show that the FG loop of the IgV domain plays a critical role in this function. B7-H3 crystallized as an unusual dimer arising from the exchange of the G strands in the IgV domains of partner molecules. This arrangement, in combination with previous reports, highlights the dynamic nature and plasticity of the immunoglobulin fold. |
