Sandbox Reserved 168

SKI proteinSKI protein

spinqualitylabelsall models Crystal Structure of human SKI, PDB ID: 1SBX Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

This Sandbox is Reserved from March 9, 2011, through May 30, 2011 for use by the course Biochemistry at Reinhardt University, Waleska, USA, taught by Irma Santoro. This reservation includes Sandbox Reserved 162 through Sandbox Reserved 168.

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BackgroundBackground

The SKI protein was first identified as an oncoprotein. An oncoprotein is one that has the potential to cause abnormal cellular proliferation if mutated or if expressed in quantitative amounts. Although, for a time the method by which the SKI protein acquired such capabilities was unknown, it was recently discovered that SKI interacts with smad after stimulation by TGF-beta. TGF-beta are proteins directly associated with proliferation and cellular differentiation, while smads are transcription factors that transduce TGF-beta members to activate transcription. SKI blocks the activation of transcription witht eh smad complexes which makes the cells resistant to the inhibitory reactions of normal growth induced by TGF-beta. Note that the stimulation of TGF-beta may cause the rapid degradation of SKI. However, after a relatively brief amount of time its expression is strongly induced. .

StructureStructure

This protein is made up of 728 amino acids <ref name="SKI protein structure"> Wilson JJ, Malakhova M, Zhang R, Joachimiak A, Hedge RS. May 2004. "Crystal Struture of the Dachshund homology domain of human SKI" Structure 12 (5):785-92. http://www.ncbi.nlm.nih.gov/pubmed/15130471>. The SKI protein maintains several domains that include the amino-terminus, a proline rich area, helix-loop-helix motifs, a cysteine/histidine-rich area, a region of basic amino acids and finally a leucine zipper-like domain. <ref name="SKI protein str."> Zheng G, Teumer J, Colmenares C, Richmond C and Stavnezer E. 1997. Oncogene. http://www.nature.com/onc/journal/v22/n20/full/1206452a.html>.