1mr1
From Proteopedia
Crystal Structure of a Smad4-Ski Complex
Overview
The Ski family of nuclear oncoproteins represses TGF-beta signaling through interactions with the Smad proteins. The crystal structure of the Smad4 binding domain of human c-Ski in complex with the MH2 domain of Smad4 reveals specific recognition of the Smad4 L3 loop region by a highly conserved interaction loop (I loop) from Ski. The Ski binding surface on Smad4 significantly overlaps with that required for binding of the R-Smads. Indeed, Ski disrupts the formation of a functional complex between the Co- and R-Smads, explaining how it could lead to repression of TGF-beta, activin, and BMP responses. Intriguingly, the structure of the Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.
About this Structure
1MR1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling., Wu JW, Krawitz AR, Chai J, Li W, Zhang F, Luo K, Shi Y, Cell. 2002 Nov 1;111(3):357-67. PMID:12419246 Page seeded by OCA on Sat May 3 01:37:04 2008
Categories: Homo sapiens | Protein complex | Chai, J. | Krawitz, A R. | Li, W. | Luo, K. | Shi, Y. | Wu, J W. | Zhang, F. | Cancer | Protein interaction | Ski | Smad | Tgf-b signaling
