Speckle-type POZ protein
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FunctionSpeckle-type POZ (pox virus and zinc finger) protein (SPOP) is an adaptor of the cullin-3-based ubiquitin ligase responsible for the degradation of oncoproteins which are overexpressed in many tumor cells[1]. SPOP forms nuclear foci after DNA damage at DNA double-strand break sites. SPOP interacts with bromodomain proteins via their MATH (Meprin And TRAP Homology) domain and regulate them. DiseaseSPOP mutations contribute to prostate cancer development by altering the steady-state levels of key components in the androgen-signaling pathway [2]. Structural highlightsThe 3D structure of SPOP MATH domain complex with bromodomain (BRD3) peptide shows the BRD3 located in the shallow groove of the MATH surface with the prostate cancer-associated mutations located at SPOP residues forming H-bonds or hydrophobic contacts with BRD3 and the endometrial-associated (uterus-associated) cancer mutations (in magenta) located far from the BRD3 binding site[3]. 3D structures of speckle-type POZ proteinSpeckle-type POZ protein 3D structures
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This page was last modified 13:50, 25 August 2022.