SH2 domains: modulators of nonreceptor tyrosine kinase activity.
|Abstract||The Src homology 2 (SH2) domain is a sequence-specific phosphotyrosine-binding module present in many signaling molecules. In cytoplasmic tyrosine kinases, the SH2 domain is located N-terminally to the catalytic kinase domain (SH1) where it mediates cellular localization, substrate recruitment, and regulation of kinase activity. Initially, structural studies established a role of the SH2 domain stabilizing the inactive state of Src family members ... [truncated at 450 characters in length]|
|Author||Filippakopoulos, Panagis; Müller, Susanne; Knapp, Stefan;|
Conformational stability and activity of p73 require a second helix in the tetramerization domain.
|Abstract||p73 and p63, the two ancestral members of the p53 family, are involved in neurogenesis, epithelial stem cell maintenance and quality control of female germ cells. The highly conserved oligomerization domain (OD) of tumor suppressor p53 is essential for its biological functions, and its structure was believed to be the prototype for all three proteins. However, we report that the ODs of p73 and p63 differ from the OD of p53 by containing an additi ... [truncated at 450 characters in length]|
|Author||Coutandin, D; Löhr, F; Niesen, F H; et al|