| Autor: |
Linhoff, Michael W., Harton, Jonathan A., Cressman, Drew E., Martin, Brian K., Ting, Jenny Pan-Yun |
| Zdroj: |
Molecular and Cellular Biology; May 2001, Vol. 21 Issue: 9 p3001-3011, 11p |
| Abstrakt: |
ABSTRACTCIITA is the master regulator of class II major histocompatibility complex gene expression. We present evidence that CIITA can self-associate via two domains: the C terminus (amino acids 700 to 1130) and the GTP-binding domain (amino acids 336 to 702). Heterotypic and homotypic interactions are observed between these two regions. Deletions within the GTP-binding domain that reduce GTP-binding and transactivation function also reduce self-association. In addition, two leucine residues in the C-terminal leucine-rich repeat region are critical for self-association as well as function. This study reveals for the first time a complex pattern of CIITA self-association. These interactions are discussed with regard to the apoptosis signaling proteins, Apaf-1 and Nod1, which share domain arrangements similar to those of CIITA. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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