Article
Three key residues underlie the differential affinity of the TGFbeta isoforms for the TGFbeta type II receptor.
Journal of molecular biology - 6 Jan 2006
De Crescenzo Gregory, Hinck Cynthia S, Shu Zhanyong, Zúñiga Jorge, Yang Junhua, Tang Yuping, Baardsnes Jason, Mendoza Valentín, Sun LuZhe, López-Casillas Fernando, O'Connor-McCourt Maureen, Hinck Andrew P
Abstract excerpt
TGFbeta1, beta2, and beta3 are 25kDa homodimeric polypeptides that play crucial non-overlapping roles in development, tumor suppression, and wound healing. They exhibit 70-82% sequence identity and transduce their signals by binding and bringing together the TGFbeta type I and type II receptors, TbetaRI and TbetaRII. TGFbeta2 differs from the other isoforms in that it binds TbetaRII weakly and is dependent upon...
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