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T Cell Immunoglobulin Mucin-3 Crystal Structure Reveals a Galectin-9-Independent Ligand-Binding Surface
- Source :
-
Immunity (10747613) . Mar2007, Vol. 26 Issue 3, p311-321. 11p. - Publication Year :
- 2007
-
Abstract
- Summary: The T cell immunoglobulin mucin (Tim) family of receptors regulates effector CD4+ T cell functions and is implicated in autoimmune and allergic diseases. Tim-3 induces immunological tolerance, and engagement of the Tim-3 immunoglobulin variable (IgV) domain by galectin-9 is important for appropriate termination of T helper 1-immune responses. The 2 Å crystal structure of the Tim-3 IgV domain demonstrated that four cysteines, which are invariant within the Tim family, form two noncanonical disulfide bonds, resulting in a surface not present in other immunoglobulin superfamily members. Biochemical and biophysical studies demonstrated that this unique structural feature mediates a previously unidentified galectin-9-independent binding process and suggested that this structural feature is conserved within the entire Tim family. The current work provided a graphic example of the relationship between sequence, structure, and function and suggested that the interplay between multiple Tim-3-binding activities contributes to the regulated assembly of signaling complexes required for effective Th1-mediated immunity. [Copyright &y& Elsevier]
- Subjects :
- *T cells
*AUTOIMMUNE diseases
*IMMUNOGLOBULINS
*PHYSICAL biochemistry
Subjects
Details
- Language :
- English
- ISSN :
- 10747613
- Volume :
- 26
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Immunity (10747613)
- Publication Type :
- Academic Journal
- Accession number :
- 24387592
- Full Text :
- https://doi.org/10.1016/j.immuni.2007.01.016