Crystal structure of the CD2-binding domain of CD58 (lymphocyte function-associated antigen 3) at 1.8-A resolution.
The binding of the cell surface molecule CD58 (formerly lymphocyte function-associated antigen 3) to its ligand, CD2, significantly increases the sensitivity of antigen recognition by T cells. This was the first heterophilic cell adhesion interaction to be discovered and is now an important paradigm...
المؤلفون الرئيسيون: | Ikemizu, S, Sparks, L, Van Der Merwe, P, Harlos, K, Stuart, D, Jones, E, Davis, S |
---|---|
التنسيق: | Journal article |
اللغة: | English |
منشور في: |
1999
|
مواد مشابهة
-
Crystal structure and binding properties of the CD2 and CD244 (2B4)-binding protein, CD48.
حسب: Evans, E, وآخرون
منشور في: (2006) -
Impact of salt bridges on the equilibrium binding and adhesion of human CD2 and CD58.
حسب: Bayas, M, وآخرون
منشور في: (2007) -
Human cell-adhesion molecule CD2 binds CD58 (LFA-3) with a very low affinity and an extremely fast dissociation rate but does not bind CD48 or CD59.
حسب: van der Merwe, P, وآخرون
منشور في: (1994) -
The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interaction.
حسب: Kearney, A, وآخرون
منشور في: (2007) -
Antigen-Independent Maturation of CD2, CD11a/CD18,CD44, and CD58 Expression on Thymic Emigrants inFetal and Postnatal Sheep
حسب: Deborah A. Witherden, وآخرون
منشور في: (1995-01-01)