1mr1

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spinqualitylabelsall models 1mr1, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of a Smad4-Ski Complex

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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.

Disease

Known diseases associated with this structure: 1p36 deletion syndrome OMIM:[164780], Juvenile polyposis/hereditary hemorrhagic telangiectasia syndrome OMIM:[600993], Pancreatic cancer OMIM:[600993], Polyposis, juvenile intestinal OMIM:[600993]

About this Structure

1MR1 is a Protein complex structure of sequences from Homo sapiens with ZN as ligand. 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

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