| Literature DB >> 23583036 |
Vladimir Vigdorovich1, Udupi A Ramagopal, Eszter Lázár-Molnár, Eliezer Sylvestre, Jun Sik Lee, Kimberly A Hofmeyer, Xingxing Zang, Stanley G Nathenson, Steven C Almo.
Abstract
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 Å 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.Entities:
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Year: 2013 PMID： 23583036 PMCID： PMC3998375 DOI： 10.1016/j.str.2013.03.003
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006