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From Proteopedia
Crystal structure of murine B7-H3 extracellular domain
Structural highlights
FunctionCD276_MOUSE Modulates T-cell-mediated immune responses and the development of acute and chronic transplant rejection. Plays a positive regulatory role in bone formation and has a dual role in the bone-immune interface. Induces antitumor immunity as it activates both acquired and innate immunity leading to natural killer cell and CD8 T-cell dependent killing of tumor cells.[1] [2] [3] [4] [5] Publication Abstract from PubMedT 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. Structure and T cell inhibition properties of B7 family member, B7-H3.,Vigdorovich V, Ramagopal UA, Lazar-Molnar E, Sylvestre E, Lee JS, Hofmeyer KA, Zang X, Nathenson SG, Almo SC Structure. 2013 May 7;21(5):707-17. doi: 10.1016/j.str.2013.03.003. Epub 2013 Apr, 11. PMID:23583036[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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